Fibril

As such, simple beam bending equations can be applied to calculate flexural strength of fibrils under ultra-low loading conditions.

[2] Unlike biopolymers, fibrils do not behave like homogeneous materials, as yield strength has been shown to vary with volume, indicating structural dependencies.

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.

[4] From a biological standpoint, water content acts as a toughening mechanism for fibril structures, allowing for higher energy absorption and greater straining capabilities.

[5] 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.

[2] A scanning electron microscope (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.

Natural materials show a combination of normally contradicting mechanical properties (softness and toughness), due to their hierarchical structures of fibrils across multiple length scales.

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.

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.

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.

The primary cell wall derives its notable tensile strength from cellulose molecules, or long-chains of glucose residues stabilized by hydrogen bonding.

In plants, these cellulose microfibrils arrange themselves into layers, formally known as lamellae, and are stabilized in the cell wall by surface, long cross-linking glycan molecules.

Coextensive in the primary cell wall to both cellulose microfibrils and complementary glycan networks, is pectin which is a polysaccharide that contains many negatively charged galacturonic acid units.

The stereoscopic arrangement of microfibrils in the cell wall create systems of turgor pressure which ultimately leads to cellular growth and expansion.

[18] 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.

These molecules form micellar structures in situ, and disulfide bridges at low pH, leading to the formation and crystallization of 200 kDa polymeric nanofibrils.

Hierarchical structure of hair in the cortex and cuticle, highlighting the scale which defines fibrils.
Structure of Collagen I fibrils
Space fill model of cellulose, prior to winding into fibrils