Advanced glycation end-products reduce collagen molecular sliding to affect collagen fibril damage mechanisms but not stiffness.

ABSTRACT: Advanced glycation end-products (AGE) contribute to age-related connective tissue damage and functional deficit. The documented association between AGE formation on collagens and the correlated progressive stiffening of tissues has widely been presumed causative, despite the lack of mechanistic understanding. The present study investigates precisely how AGEs affect mechanical function of the collagen fibril--the supramolecular functional load-bearing unit within most tissues. We employed synchrotron small-angle X-ray scattering (SAXS) and carefully controlled mechanical testing after introducing AGEs in explants of rat-tail tendon using the metabolite methylglyoxal (MGO). Mass spectrometry and collagen fluorescence verified substantial formation of AGEs by the treatment. Associated mechani

SUBMITTER: Fessel G 

PROVIDER: S-EPMC4217736 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature