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subsection</span> </button> <ul id="toc-Structure_and_mechanics-sublist" class="vector-toc-list"> <li id="toc-Contributions_to_mechanical_properties_of_biomaterials" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Contributions_to_mechanical_properties_of_biomaterials"> <div class="vector-toc-text"> <span class="vector-toc-numb">1.1</span> <span>Contributions to mechanical properties of biomaterials</span> </div> </a> <ul id="toc-Contributions_to_mechanical_properties_of_biomaterials-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Natural_processes" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Natural_processes"> <div class="vector-toc-text"> <span class="vector-toc-numb">1.2</span> <span>Natural processes</span> </div> </a> <ul id="toc-Natural_processes-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-In_animals" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#In_animals"> <div class="vector-toc-text"> <span class="vector-toc-numb">2</span> <span>In animals</span> </div> </a> <button aria-controls="toc-In_animals-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle In animals subsection</span> </button> <ul id="toc-In_animals-sublist" class="vector-toc-list"> <li id="toc-Collagen" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Collagen"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.1</span> <span>Collagen</span> </div> </a> <ul id="toc-Collagen-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Actin_and_myosin" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Actin_and_myosin"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.2</span> <span>Actin and myosin</span> </div> </a> <ul id="toc-Actin_and_myosin-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Elastin_and_keratin" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Elastin_and_keratin"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.3</span> <span>Elastin and keratin</span> </div> </a> <ul id="toc-Elastin_and_keratin-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Resilin_and_spider_silk" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Resilin_and_spider_silk"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.4</span> <span>Resilin and spider silk</span> </div> </a> <ul id="toc-Resilin_and_spider_silk-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-In_plants" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#In_plants"> <div class="vector-toc-text"> <span 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id="siteSub" class="noprint">From Wikipedia, the free encyclopedia</div> </div> <div id="contentSub"><div id="mw-content-subtitle"></div></div> <div id="mw-content-text" class="mw-body-content"><div class="mw-content-ltr mw-parser-output" lang="en" dir="ltr"><div class="shortdescription nomobile noexcerpt noprint searchaux" style="display:none">Structural material present in almost all organic life</div> <figure typeof="mw:File/Thumb"><a href="/wiki/File:Hierarchical_structure_of_hair_in_the_cortex_and_cuticle.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/5/55/Hierarchical_structure_of_hair_in_the_cortex_and_cuticle.png/399px-Hierarchical_structure_of_hair_in_the_cortex_and_cuticle.png" decoding="async" width="399" height="157" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/5/55/Hierarchical_structure_of_hair_in_the_cortex_and_cuticle.png/599px-Hierarchical_structure_of_hair_in_the_cortex_and_cuticle.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/5/55/Hierarchical_structure_of_hair_in_the_cortex_and_cuticle.png/798px-Hierarchical_structure_of_hair_in_the_cortex_and_cuticle.png 2x" data-file-width="8660" data-file-height="3414" /></a><figcaption>Hierarchical structure of <a href="/wiki/Hair" title="Hair">hair</a> in the cortex and cuticle, highlighting the scale which defines fibrils.</figcaption></figure> <p><b>Fibrils</b> (from <a href="/wiki/Latin_language" class="mw-redirect" title="Latin language">Latin</a> <i> fibra</i><sup id="cite_ref-1" class="reference"><a href="#cite_note-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup>) are structural biological materials found in nearly all living <a href="/wiki/Organism" title="Organism">organisms</a>. Not to be confused with <a href="/wiki/Fibers" class="mw-redirect" title="Fibers">fibers</a> or <a href="/wiki/Protein_filament" title="Protein filament">filaments</a>, fibrils tend to have diameters ranging from 10 to 100 nanometers (whereas fibers are micro to milli-scale structures and filaments have diameters approximately 10–50 nanometers in size). Fibrils are not usually found alone but rather are parts of greater hierarchical structures commonly found in biological systems. Due to the prevalence of fibrils in biological systems, their study is of great importance in the fields of <a href="/wiki/Microbiology" title="Microbiology">microbiology</a>, <a href="/wiki/Biomechanics" title="Biomechanics">biomechanics</a>, and <a href="/wiki/Materials_science" title="Materials science">materials science</a>. </p> <style data-mw-deduplicate="TemplateStyles:r886046785">.mw-parser-output .toclimit-2 .toclevel-1 ul,.mw-parser-output .toclimit-3 .toclevel-2 ul,.mw-parser-output .toclimit-4 .toclevel-3 ul,.mw-parser-output .toclimit-5 .toclevel-4 ul,.mw-parser-output .toclimit-6 .toclevel-5 ul,.mw-parser-output .toclimit-7 .toclevel-6 ul{display:none}</style><div class="toclimit-3"><meta property="mw:PageProp/toc" /></div> <div class="mw-heading mw-heading2"><h2 id="Structure_and_mechanics">Structure and mechanics</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fibril&action=edit&section=1" title="Edit section: Structure and mechanics"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Fibrils are composed of linear <a href="/wiki/Biopolymers" class="mw-redirect" title="Biopolymers">biopolymers</a>, and are characterized by rod-like structures with high length-to-diameter ratios. They often spontaneously arrange into helical structures. In <a href="/wiki/Biomechanics" title="Biomechanics">biomechanics</a> problems, fibrils can be characterized as classical beams with a roughly circular cross-sectional area on the nanometer scale. As such, simple <a href="/wiki/Beam_bending" class="mw-redirect" title="Beam bending">beam bending</a> equations can be applied to calculate <a href="/wiki/Flexural_strength" title="Flexural strength">flexural strength</a> of fibrils under ultra-low loading conditions. Like most biopolymers, stress-strain relationships of fibrils tend to show a characteristic toe-heel region before a linear, <a href="/wiki/Hooke%27s_Law" class="mw-redirect" title="Hooke's Law">elastic region</a>.<sup id="cite_ref-:2_2-0" class="reference"><a href="#cite_note-:2-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> Unlike biopolymers, fibrils do not behave like homogeneous materials, as yield strength has been shown to vary with volume, indicating structural dependencies.<sup id="cite_ref-3" class="reference"><a href="#cite_note-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Hydrate" title="Hydrate">Hydration</a> has been shown to produce a noticeable effect in the mechanical properties of fibrillar materials. The presence of water (an aldehyde) has been shown to decrease the stiffness of collagen fibrils, as well as increase their rate of stress relaxation and strength.<sup id="cite_ref-4" class="reference"><a href="#cite_note-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> From a biological standpoint, water content acts as a toughening mechanism for fibril structures, allowing for higher energy absorption and greater straining capabilities. </p><p>Fibrils mechanical strengthening properties originate at the molecular level. The forces distributed in the fiber are <a href="/wiki/Tensile_load" class="mw-redirect" title="Tensile load">tensile load</a> carried by the fibril and <a href="/wiki/Shear_force" title="Shear force">shear forces</a> felt due to interaction with other fibril molecules. The fracture strength of individual collagen molecules is as a result controlled by covalent chemistry between molecules. The shear strength between two collagen molecules is controlled by weak dispersive and <a href="/wiki/Hydrogen_bond" title="Hydrogen bond">hydrogen bond</a> interactions and by some molecular covalent <a href="/wiki/Cross-link" title="Cross-link">crosslinks</a>. Slip in the system occur when these intermolecular bonds face an applied stress greater than their interaction strength.<sup id="cite_ref-5" class="reference"><a href="#cite_note-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> Intermolecular bonds breaking do not immediately lead to failure, in contrast they play an essential role in energy dissipation that lower the stress felt overall by the material and enable it to withstand fracture.  These bonds, often hydrogen bonding and dispersive <a href="/wiki/Van_der_Waals_force" title="Van der Waals force">Van der Waals</a> interactions, act as “sacrificial” bonds, existing for the purpose of lowering stress in the network. Molecular covalent crosslinks also play a key role in the formation of fibril networks. While crosslinking molecules can lead to strong structures, too much crosslinking in biopolymer networks are more likely to fracture as the network is not able to dissipate the energy, leading to a material that is strong but not tough. This is observed in dehydrated or aged collagen, explaining why with age human tissues become more <a href="/wiki/Brittleness" title="Brittleness">brittle</a>.<sup id="cite_ref-6" class="reference"><a href="#cite_note-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> </p><p>Differences in structure between fibrils of different origin is typically determined by x-ray diffraction.<sup id="cite_ref-:2_2-1" class="reference"><a href="#cite_note-:2-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> A <a href="/wiki/Scanning_electron_microscope" title="Scanning electron microscope">scanning electron microscope</a> (SEM) can be used to observe specific details on larger fibril species such as the characteristic 67 nm bands in collagen, but often is not fine enough to determine the full structure. </p> <div class="mw-heading mw-heading3"><h3 id="Contributions_to_mechanical_properties_of_biomaterials">Contributions to mechanical properties of biomaterials</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fibril&action=edit&section=2" title="Edit section: Contributions to mechanical properties of biomaterials"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Natural materials show a combination of normally contradicting mechanical properties (<a href="/wiki/Softness" class="mw-redirect" title="Softness">softness</a> and <a href="/wiki/Toughness" title="Toughness">toughness</a>), due to their hierarchical structures of fibrils across multiple length scales.<sup id="cite_ref-:3_7-0" class="reference"><a href="#cite_note-:3-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> These fibrils are often oriented in a single direction, leading to <a href="/wiki/Anisotropy" title="Anisotropy">anisotropic</a> mechanical response in the resulting biocomposite material.<sup id="cite_ref-:4_8-0" class="reference"><a href="#cite_note-:4-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> This is a prime advantage as most of these materials withstand stresses in a single direction, and so a higher yield and fracture stress in the direction of the applied stress ensures the material structural integrity. Macro, micro, and nano fibrils enable the material to resist fracture through a series of fracture resistance mechanisms: </p> <ol><li>Fibrillar sliding, or the process of shear as load is applied, enabling <a href="/wiki/Plasticity_(physics)" title="Plasticity (physics)">plasticity</a></li> <li>Fibril bridging across the region of a crack</li> <li>Crack deflection at the tip of crack, where stress concentration can lead to further propagation and eventual failure.<sup id="cite_ref-:3_7-1" class="reference"><a href="#cite_note-:3-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup></li></ol> <p>These mechanisms work together to resist fracture, allowing these materials to withstand millions of cycles of load without failure, essential for mobile living beings. Another mechanical advantage of biopolymers is their ability to be strained, resulting from the existence of strong fibrillar structures in a more compliant matrix material. The good deformability of interfacial matrices plays a key role in allowing for reorientation of constituents during deformation.<sup id="cite_ref-:4_8-1" class="reference"><a href="#cite_note-:4-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> </p> <style data-mw-deduplicate="TemplateStyles:r1236090951">.mw-parser-output .hatnote{font-style:italic}.mw-parser-output div.hatnote{padding-left:1.6em;margin-bottom:0.5em}.mw-parser-output .hatnote i{font-style:normal}.mw-parser-output .hatnote+link+.hatnote{margin-top:-0.5em}@media print{body.ns-0 .mw-parser-output .hatnote{display:none!important}}</style><div role="note" class="hatnote navigation-not-searchable">Main article: <a href="/wiki/Fibrillogenesis" title="Fibrillogenesis">Fibrillogenesis</a></div> <p><a href="/wiki/Fibrillogenesis" title="Fibrillogenesis">Fibrillogenesis</a> is the expansion of fine fibrils which is common in <a href="/wiki/Collagen" title="Collagen">collagen</a> fibers of <a href="/wiki/Connective_tissue" title="Connective tissue">connective tissue</a>. The definite mechanisms of fibrillogenesis are still unknown, although many hypotheses resulting from basic research help discover many possible mechanisms. In early experiments, collagen I could be distilled from tissues and recombined into fibrils with controlling the solutions. Later studies help understand the composition and structure of binding sites on the collagen monomers. Collagen is synthesized as a soluble precursor, procollagen, which supports collagen self-assembly. Since collagen fibrils have almost 50 binding components in vivo, the definite requirement to generate fibrillogenesis in vivo is still cryptic.<sup id="cite_ref-9" class="reference"><a href="#cite_note-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> </p><p>With acidic or saline solution, collagen can be extracted from tissues and rearrange into fibril by changing temperature or pH value.<sup id="cite_ref-10" class="reference"><a href="#cite_note-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> Experiments discovered attractive force between collagen monomers which helps the rearrangement.<sup id="cite_ref-11" class="reference"><a href="#cite_note-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> Collagen serves as a precursor, procollagen, in synthesizing reaction, which identifies self-polymerization of collagen. </p> <div class="mw-heading mw-heading3"><h3 id="Natural_processes">Natural processes</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fibril&action=edit&section=3" title="Edit section: Natural processes"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>There are over 30 collagens in nature that are similar in chemical composition but differ in terms of crystal structure. By far, <a href="/wiki/Collagen_I" class="mw-redirect" title="Collagen I">collagen I</a> and II are the most abundant. They initiatively form fibrils in vitro, while fibronectin, fibronectin-binding, collagen-binding integrins and collagen V are essential for collagen I forming and collagen XI for collagen II forming. Therefore, cellular mechanisms play key role in the protein self-assembly process. </p> <div class="mw-heading mw-heading2"><h2 id="In_animals">In animals</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fibril&action=edit&section=4" title="Edit section: In animals"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <div class="mw-heading mw-heading3"><h3 id="Collagen">Collagen</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fibril&action=edit&section=5" title="Edit section: Collagen"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Main article: <a href="/wiki/Collagen" title="Collagen">Collagen</a></div> <figure typeof="mw:File/Thumb"><a href="/wiki/File:Collagen_biosynthesis_(en).png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/2/2f/Collagen_biosynthesis_%28en%29.png/319px-Collagen_biosynthesis_%28en%29.png" decoding="async" width="319" height="209" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/2/2f/Collagen_biosynthesis_%28en%29.png/479px-Collagen_biosynthesis_%28en%29.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/2/2f/Collagen_biosynthesis_%28en%29.png/638px-Collagen_biosynthesis_%28en%29.png 2x" data-file-width="701" data-file-height="459" /></a><figcaption>Structure of Collagen I fibrils</figcaption></figure> <p><a href="/wiki/Collagen" title="Collagen">Collagen</a> is the major structural protein outside cells in many connective tissues of animals.<sup id="cite_ref-12" class="reference"><a href="#cite_note-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> As the primary component of connective tissue, it has the largest amount among protein in mammals, occupying 25% to 35% of all protein content in the body. </p><p>The fibrils in collagen are packed in a crimp structure. The stress/strain curve of collagen, such as tendon, can be subdivided into several regions. The region of small strains, "toe" region, corresponds to the removal of a macroscopic crimp, uncrimping, in the collagen fibrils, visible in light microscope. At larger strains, "heel" and "linear" region, there's no further structural change visible. </p><p><a href="/wiki/Tropocollagen" class="mw-redirect" title="Tropocollagen">Tropocollagen</a> is the molecular component fiber, consisting of three left handed polypeptide chains (red, green, blue) coiled around each other, forming a right-handed triple helix. </p> <div class="mw-heading mw-heading3"><h3 id="Actin_and_myosin"><a href="/wiki/Actin" title="Actin">Actin</a> and <a href="/wiki/Myosin" title="Myosin">myosin</a></h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fibril&action=edit&section=6" title="Edit section: Actin and myosin"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Muscles contract and stretch via the steerable sliding/grasping of the <a href="/wiki/Myosin" title="Myosin">myosin</a> interacting with <a href="/wiki/Actin" title="Actin">actin</a> fibers. Actin consists of two polypeptides in a helix and myosin has a small heart-shaped structure, cross-bridge. The bind and unbind processes of cross-bridge attaching on actin filament help relative movement of these collagens and hence the whole muscle. </p> <div class="mw-heading mw-heading3"><h3 id="Elastin_and_keratin"><a href="/wiki/Elastin" title="Elastin">Elastin</a> and <a href="/wiki/Keratin" title="Keratin">keratin</a></h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fibril&action=edit&section=7" title="Edit section: Elastin and keratin"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Elastin" title="Elastin">Elastin</a> is a fibrous protein common in various soft tissues, like skin, blood vessels and lung tissue. Each monomer connects with each other, forming a 3D network, with ability to endure over 200% strain before deformation.<sup id="cite_ref-13" class="reference"><a href="#cite_note-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup> </p><p><a href="/wiki/Keratin" title="Keratin">Keratin</a> is a structural protein mainly found in hair, nails, hooves, horns, quills.<sup id="cite_ref-14" class="reference"><a href="#cite_note-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup> Basically keratin is formed by polypeptide chains, which coil into α-helices with sulfur cross-links or bond into β-sheets linked by hydrogen bonding. β-keratin, which is tougher than α-conformation, is more common in birds and reptiles. </p> <div class="mw-heading mw-heading3"><h3 id="Resilin_and_spider_silk"><a href="/wiki/Resilin" title="Resilin">Resilin</a> and <a href="/wiki/Spider_silk" title="Spider silk">spider silk</a></h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fibril&action=edit&section=8" title="Edit section: Resilin and spider silk"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Resilin" title="Resilin">Resilin</a> is an elastomeric insect protein, consisting of both α-helices and β-sheets structure.<sup id="cite_ref-15" class="reference"><a href="#cite_note-15"><span class="cite-bracket">[</span>15<span class="cite-bracket">]</span></a></sup> It is one of the most resilient protein in nature. It has a low stiffness ~0.6MPa but a high energy restoring percentage ~98%, and efficiently helps flying insects to flap wings or fleas to jump. </p><p><a href="/wiki/Spider_silk" title="Spider silk">Spider silk</a> fibril is composed of stiff crystallized β-sheets structure, responsible for strength, and amorphous matrix surrounding, improving toughness and elongation ability.<sup id="cite_ref-16" class="reference"><a href="#cite_note-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> It has exceptionally high tensile strength and ductility, with respectively low density, compared to other natural fibril. Its feature varies from different kinds of spider for different utility. </p> <div class="mw-heading mw-heading2"><h2 id="In_plants">In plants</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fibril&action=edit&section=9" title="Edit section: In plants"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <div class="mw-heading mw-heading3"><h3 id="Cellulose">Cellulose</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fibril&action=edit&section=10" title="Edit section: Cellulose"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Main article: <a href="/wiki/Cellulose" title="Cellulose">Cellulose</a></div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Cellulose_spacefilling_model.jpg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/a/a3/Cellulose_spacefilling_model.jpg/220px-Cellulose_spacefilling_model.jpg" decoding="async" width="220" height="86" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/a/a3/Cellulose_spacefilling_model.jpg/330px-Cellulose_spacefilling_model.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/a/a3/Cellulose_spacefilling_model.jpg/440px-Cellulose_spacefilling_model.jpg 2x" data-file-width="1070" data-file-height="419" /></a><figcaption>Space fill model of cellulose, prior to winding into fibrils</figcaption></figure> <p>The primary cell wall derives its notable tensile strength from cellulose molecules, or long-chains of glucose residues stabilized by <a href="/wiki/Hydrogen_bonding" class="mw-redirect" title="Hydrogen bonding">hydrogen bonding</a>.<sup id="cite_ref-:0_17-0" class="reference"><a href="#cite_note-:0-17"><span class="cite-bracket">[</span>17<span class="cite-bracket">]</span></a></sup> Cellulose chains are observed to align in overlapping parallel arrays, with the similar polarity forming a cellulose microfibril. In plants, these cellulose microfibrils arrange themselves into layers, formally known as <a href="/w/index.php?title=Lamellae_(disambiguation)&action=edit&redlink=1" class="new" title="Lamellae (disambiguation) (page does not exist)">lamellae</a>, and are stabilized in the cell wall by surface, long cross-linking <a href="/w/index.php?title=Glycan_molecules&action=edit&redlink=1" class="new" title="Glycan molecules (page does not exist)">glycan molecules</a>. Glycan molecules increase the complexity of the potential networks plant-based cellulose can configure itself into. Coextensive in the primary cell wall to both cellulose microfibrils and complementary glycan networks, is <a href="/wiki/Pectin" title="Pectin">pectin</a> which is a polysaccharide that contains many negatively charged galacturonic acid units.<sup id="cite_ref-:0_17-1" class="reference"><a href="#cite_note-:0-17"><span class="cite-bracket">[</span>17<span class="cite-bracket">]</span></a></sup> Additionally, cellulose microfibrils also contribute to the shape of the plant via controlled-cell expansion. The stereoscopic arrangement of microfibrils in the cell wall create systems of <a href="/wiki/Turgor_pressure" title="Turgor pressure">turgor pressure</a> which ultimately leads to cellular growth and expansion. Cellulose microfibrils are unique matrix macromolecules, in that they are assembled by cellulose synthase enzymes located on the extracellular surface of the plasma membrane.<sup id="cite_ref-:0_17-2" class="reference"><a href="#cite_note-:0-17"><span class="cite-bracket">[</span>17<span class="cite-bracket">]</span></a></sup> It is believed that the plant can “anticipate their future morphology by controlling the orientation of microfibrils” by a mechanism where cellulose microfibrils are arranged atop a cortical array of microtubules. </p> <div class="mw-heading mw-heading3"><h3 id="Amylose">Amylose</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fibril&action=edit&section=11" title="Edit section: Amylose"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Main article: <a href="/wiki/Amylose" title="Amylose">Amylose</a></div> <p>Stirring of a given sample of amylose is said to form <a href="/w/index.php?title=Fibrillar_crystals&action=edit&redlink=1" class="new" title="Fibrillar crystals (page does not exist)">fibrillar crystals</a> which are said to precipitate out of the mother liquor. These long fibrils can be imaged using electron microscopy revealing transverse striations resembling a <a href="/wiki/Shish-kebab" class="mw-redirect" title="Shish-kebab">shish-kebab</a>. <sup class="noprint Inline-Template Template-Fact" style="white-space:nowrap;">[<i><a href="/wiki/Wikipedia:Citation_needed" title="Wikipedia:Citation needed"><span title="This claim needs references to reliable sources. (May 2017)">citation needed</span></a></i>]</sup> Amylose fibrils are categorized with having one of two morphologies: ones with small rodlike fibrils and others with lath-shaped crystals. </p> <div class="mw-heading mw-heading3"><h3 id="Wood">Wood</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fibril&action=edit&section=12" title="Edit section: Wood"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The fibrillar structure of wood is said to play a significant role in both the mechanical stability and ability of wood to possess channels to transport minerals and water. Sprucewood (Picea abies), among others, are reported to possess cellulose fibrils with a normalized diameter of 2.5 nm. There is also a reported link between the age of the wood and the spiral angle of the fibrils with respect to the longitudinal direction. Earlywood is said to have a consistent 4.6 ± 0.6° rest angle, whereas latewood is said to have a transition region from 4.6° to 19.8 ± 0.7°.<sup id="cite_ref-:1_18-0" class="reference"><a href="#cite_note-:1-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup> In latewood, the two spiral angle regions of cellulose fibrils are not continuous, meaning that there are two independent tracheid structures in “older” trees meeting different mechanical requirements. Moreover, longitudinally oriented fibrils improve tensile strength, whereas the addition of 20° tilted fibrils, exclusive to latewood tracheids, provides stability against compression.<sup id="cite_ref-:1_18-1" class="reference"><a href="#cite_note-:1-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Biomimicry_and_fibrils">Biomimicry and fibrils</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fibril&action=edit&section=13" title="Edit section: Biomimicry and fibrils"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <div class="mw-heading mw-heading3"><h3 id="Self-cleaning_properties">Self-cleaning properties</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fibril&action=edit&section=14" title="Edit section: Self-cleaning properties"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>In order to mimic the strong adhesion, easy detachment, and self-cleaning properties of a <a href="/w/index.php?title=Gecko_toe_pad&action=edit&redlink=1" class="new" title="Gecko toe pad (page does not exist)">gecko toe pad</a>, a fibrillar-based adhesive can be created. These performance features stem from the underlying hierarchical structure which consists of a million microfibrils called <a href="/wiki/Setae" class="mw-redirect" title="Setae">setae</a> which further consists of billions of nano-sized branches called <a href="/wiki/Spatulae_(biology)" class="mw-redirect" title="Spatulae (biology)">spatulae</a>. </p><p>Mimicking this phenomenon involves four distinct design steps:<sup id="cite_ref-19" class="reference"><a href="#cite_note-19"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup> </p> <ol><li>Making a vertically aligned micro-/nano- fibrillar arrays</li> <li>Creating various tip shapes</li> <li>Including anisotropic geometry</li> <li>Building hierarchy.</li></ol> <div class="mw-heading mw-heading3"><h3 id="A_mature_bone_matrix">A mature bone matrix</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fibril&action=edit&section=15" title="Edit section: A mature bone matrix"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>In order to mimic a mature bone matrix, self-assembled fibrils can be used to align a given mineral matrix. This is accomplished using a self-assembling molecule with a hydrophobic alkyl tail and a hydrophilic oligopeptide head. These molecules form micellar structures in situ, and disulfide bridges at low pH, leading to the formation and crystallization of 200 kDa polymeric nanofibrils.<sup class="noprint Inline-Template Template-Fact" style="white-space:nowrap;">[<i><a href="/wiki/Wikipedia:Citation_needed" title="Wikipedia:Citation needed"><span title="This claim needs references to reliable sources. (May 2017)">citation needed</span></a></i>]</sup> The mineral matrix ultimately interacts with the synthetic fibril via a phosphoserine residue which results in mineral nucleation and growth. </p> <div class="mw-heading mw-heading2"><h2 id="See_also">See also</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fibril&action=edit&section=16" title="Edit section: See also"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a href="/wiki/Fibre" class="mw-redirect" title="Fibre">Fibre</a></li> <li><a href="/wiki/Microfibril" title="Microfibril">Microfibril</a></li> <li><a href="/wiki/Myofibril" title="Myofibril">Myofibril</a></li> <li><a href="/wiki/Neurofibril" class="mw-redirect" title="Neurofibril">Neurofibril</a></li> <li><a href="/wiki/Fibrillogenesis" title="Fibrillogenesis">Fibrillogenesis</a></li> <li><a href="/wiki/Protein_filament" title="Protein filament">Protein filament</a></li></ul> <div class="mw-heading mw-heading2"><h2 id="References">References</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Fibril&action=edit&section=17" title="Edit section: References"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1239543626">.mw-parser-output .reflist{margin-bottom:0.5em;list-style-type:decimal}@media screen{.mw-parser-output .reflist{font-size:90%}}.mw-parser-output .reflist .references{font-size:100%;margin-bottom:0;list-style-type:inherit}.mw-parser-output .reflist-columns-2{column-width:30em}.mw-parser-output .reflist-columns-3{column-width:25em}.mw-parser-output .reflist-columns{margin-top:0.3em}.mw-parser-output .reflist-columns ol{margin-top:0}.mw-parser-output .reflist-columns li{page-break-inside:avoid;break-inside:avoid-column}.mw-parser-output .reflist-upper-alpha{list-style-type:upper-alpha}.mw-parser-output .reflist-upper-roman{list-style-type:upper-roman}.mw-parser-output .reflist-lower-alpha{list-style-type:lower-alpha}.mw-parser-output .reflist-lower-greek{list-style-type:lower-greek}.mw-parser-output .reflist-lower-roman{list-style-type:lower-roman}</style><div class="reflist"> <div class="mw-references-wrap mw-references-columns"><ol class="references"> <li id="cite_note-1"><span class="mw-cite-backlink"><b><a href="#cite_ref-1">^</a></b></span> <span class="reference-text"><style data-mw-deduplicate="TemplateStyles:r1238218222">.mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"\"""\"""'""'"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free.id-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/6/65/Lock-green.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-limited.id-lock-limited a,.mw-parser-output .id-lock-registration.id-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/d/d6/Lock-gray-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-subscription.id-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/a/aa/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/4/4c/Wikisource-logo.svg")right 0.1em center/12px no-repeat}body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-free a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-limited a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-registration a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-subscription a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .cs1-ws-icon a{background-size:contain;padding:0 1em 0 0}.mw-parser-output .cs1-code{color:inherit;background:inherit;border:none;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;color:var(--color-error,#d33)}.mw-parser-output .cs1-visible-error{color:var(--color-error,#d33)}.mw-parser-output .cs1-maint{display:none;color:#085;margin-left:0.3em}.mw-parser-output .cs1-kern-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right{padding-right:0.2em}.mw-parser-output .citation .mw-selflink{font-weight:inherit}@media screen{.mw-parser-output .cs1-format{font-size:95%}html.skin-theme-clientpref-night .mw-parser-output .cs1-maint{color:#18911f}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .cs1-maint{color:#18911f}}</style><cite class="citation web cs1"><a rel="nofollow" class="external text" href="http://www.etymonline.com/index.php?term=fibril">"Online Etymology Dictionary"</a>. <i>www.etymonline.com</i><span class="reference-accessdate">. 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