Жұқа Талшықтар және Биологиялық Құрылымдар

Thin Fibre

Fibrils (from the Latin fibra) are structural biological materials found in nearly all living organisms. Not to be confused with fibers or filaments, fibrils tend to have diameters ranging from 10–100 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 microbiology, biomechanics, and materials science.

There are over 30 collagens in nature that are similar in chemical composition but differ in terms of crystal structure. By far, collagen I 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.

Collagen is the major structural protein outside cells in many connective tissues of animals. 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. 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. Tropocollagen 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.

Muscles contract and stretch via the steerable sliding/grasping of the myosin interacting with actin 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.

Elastin 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. Keratin is a structural protein mainly found in hair, nails, hooves, horns, quills. 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.

Resilin is an elastomeric insect protein, consisting of both α helices and β sheets structure. 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. Spider silk fibril is composed of stiff crystallized β sheets structure, responsible for strength, and amorphous matrix surrounding, improving toughness and elongation ability. 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.

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. The mineral matrix ultimately interacts with the synthetic fibril via a phosphoserine residue which results in mineral nucleation and growth.