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Determination of the number of crosslinks in collagens from mechanical properties of swollen fibers
Author(s) -
Honda Ichiro,
Arai Kozo
Publication year - 1996
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/(sici)1097-4628(19961205)62:10<1577::aid-app9>3.0.co;2-l
Subject(s) - polymer science , materials science , composite material , polymer chemistry , chemistry
A method for the determination of crosslink density for collagen fibers was proposed. The number of interchain crosslinkages in whale ligament and rat‐tail tendon was estimated by applying an usual rubber elasticity theory. Collagen fibers swollen in a solution composed of equal volumes of 8 M LiBr aqueous solution and diethylene glycol monoalkyl ether showed a typical rubber elasticity. The energy components to total retractive forces were similar in order in magnitude for crosslinked natural rubbers, namely, below 0.3. It was found that no intermolecular crosslinkage occurs between tropocollagen molecules in tendon from a 2‐month‐old rat, while there are about 12 crosslinking sites per molecule in tendon from a 10‐month‐old rat and 15 sites in whale ligament. The number, type, and crosslinking sites in the tendon crosslinked with 1,3‐bis(vinylsulfonyl)‐2‐propanol is also discussed. © 1996 John Wiley & Sons, Inc.