Collagen is the oldest and most abundant extracellular matrix protein that has found many applications in food, cosmetic, pharmaceutical, and biomedical industries First, an overview of the family of collagens and their respective structures, conformation, and biosynthesis is provided The advances and shortfalls of various collagen preparations (eg, mammalian/marine extracted collagen, cell-produced collagens, recombinant collagens, and collagen-like peptides) and crosslinking technologies (eg, chemical, physical, and biological) are then critically discussed Subsequently, an array of structural, thermal, mechanical, biochemical, and biological assays is examined, which are developed to analyze and characterize collagenous structures Lastly, a comprehensive review is provided on how advances in engineering, chemistry, and biology have enabled the development of bioactive, 3D structures (eg, tissue grafts, biomaterials, cell-assembled tissue equivalents) that closely imitate native supramolecular assemblies and have the capacity to deliver in a localized and sustained manner viable cell populations and/or bioactive/therapeutic molecules Clearly, collagens have a long history in both evolution and biotechnology and continue to offer both challenges and exciting opportunities in regenerative medicine as nature's biomaterial of choice

/pdf/the-collagen-suprafamily-from-biosynthesis-to-advanced-19x5x1lvm2.pdf

The Collagen Suprafamily: From Biosynthesis to Advanced Biomaterial Development

Collagen fibril formation in vitro. The role of the nonhelical terminal regions.

Extraction and characterization of collagen with or without telopeptides from chicken skin

Protein adducts as biomarkers of human carcinogen exposure.

Heat precipitation fibril formation in collagen solutions depends upon the prior thermal history of the solution. Collagen solutions were heat precipitated to various extents at 30°C, cooled, and then brought to a second precipitation. Kinetic analysis of the secondary precipitation demonstrated that only the nucleation phase of the precipitation was affected, not the fibril growth phase. Thermal history, or memory, is thus related to the formation of low-temperature-stable nuclei. A range of nuclei sizes is evident, supporting the concept of a homogeneous nucleation process. Schiffs base formation and establishment of cross-linkages play no role in the in vitro nucleation: thiosemicarbazide treated collagen behaves identically to untreated collagen in kinetics of assembly to fibrils. Low-temperature-stable nuclei formed at neutral pH are dissociated in the cold in acetic acid at pH 4. Pronase and pepsin susceptible molecular end regions are important in establishing the low-temperature-stable nuclei. Pronase treatment completely abolishes the acquisition of memory of prior thermal history in collagen solutions. We speculate that biological control mechanisms for fibril formation in vivo relate to specific interactions between non-helical, enzyme susceptible regions on collagen molecules.

Characterization of nuclei in in vitro collagen fibril formation.

1. Collagen was extracted from chick skin with dilute acetic acid followed by dilute acetic acid containing pepsin. 2. The solubilized collagens were purified and portions subjected to further digestion by pepsin. 3. This treatment decreased the aldehyde content but contamination by hexosamine was not diminished. 4. Pepsin treatment converted practically all the acid-soluble collagen into monomeric subunits (α-chains), but the pepsinsolubilized material retained a significant amount of higher subunits (β- and γ-chains). 5. Treatment lowered the rate of fibrillogenesis by acid-soluble collagen, but was without effect on pepsin-solubilized collagen.

/pdf/pepsin-treatment-of-avian-skin-collagen-effects-on-4psduzcqcu.pdf

Pepsin treatment of avian skin collagen. Effects on solubility, subunit composition and aggregation properties.

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Pepsin treatment of avian skin collagen. Effects on solubility, subunit composition and aggregation properties.