Effect of physical crosslinking methods on collagen-fiber durability in proteolytic solutions

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Abstract
We previously demonstrated that ultraviolet (UV) or dehydrothermal (DHT) crosslinking partially denatured fibers extruded from an insoluble type I collagen dispersion. In this study denaturation effects were evaluated by measuring collagen-fiber sensitivity to trypsin. Shrinkage-temperature measurements and sensitivity to collagenase served as indices of crosslinking. UV or DHT crosslinking increased the collagen-fiber shrinkage temperature, resistance to degradation in collagenase, and durability under load in collagenase. However, in trypsin solutions, solubility was significantly increased for UV (≈11%) or DHT (≈15%) crosslinked fibers compared with uncrosslinked fibers (≈4%). Size-exclusion chromatography indicated that no intact collagen α-chains were present in the soluble fraction of fibers exposed to trypsin (MW in vivo. © 1996 John Wiley & Sons, Inc.

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