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Hydrothermal stability of collagen and crosslink topology
Author(s) -
Ghosh Santibrata
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.2_supplement.279
Subject(s) - hydrothermal circulation , stability (learning theory) , topology (electrical circuits) , chemical engineering , chemistry , materials science , computer science , mathematics , engineering , combinatorics , machine learning
Recent work has increased our understanding about how the nonhelical regions (NC) of collagen facilitate the alignment of the chains in the triple helix. However, the topology responsible for chain recognition is still not clear. Crosslinks found in vivo have been characterized and used in aligning the chains for structural stability. Further insight may be obtained from in‐vitro crosslinking or otherwise stabilization of collagen as had been used in the age old technology of tanning. We have investigated the physico‐chemical properties of collagen, native and tanned, using electroosmosis for surface charge, swelling and shrinkage/melting (temperature Tm and extent) for hydrothermal stability. Even about one formaldehyde induced crosslink per collagen not only raises the Tm but on cooling the native dimension is largely recovered. The crosslink has to be at a unique site inside the helix for such a regeneration. The more efficient chrome tanning (CT) may raise the Tm, putatively by reacting at NC carboxylic sites reducing the swelling; this may explain why CT, while showing a much higher Tm, does not enable similar recovery of dimension on cooling. Oil tanning involves the formation of peroxides and aldehydes and works like formaldehyde. The key site of aldehyde induced crosslink, whether between two (lysine) groups or between three groups from three chains forming a merodesmosine like structure, remains to be seen.