Processing of type I collagen gels using nonenzymatic glycation.
This study focuses on the development of a novel method of nonenzymatic glycation of fibrillar collagen gels. In contrast to previous studies in which type I collagen gels were glycated in the solid state, this study presents a method for glycation in solution. The type I collagen in solution or gels was exposed to a range of ribose concentrations from 0 to 250 mM. The binding of ribose to collagen was documented using Fourier transform infrared (FTIR) spectroscopy. formation of advanced glycation end products (AGEs) was quantified by fluorescence measurement. The bulk compressive modulus and viscoelastic time constant of processed gels were determined in stress relaxation studies. Both methods of glycation enhanced ribose addition and AGE formation in a dose-dependent manner, with glycation in the gel state being more efficient. Both methods enhanced mechanical properties similarly, with 250 mM ribose treatment resulting in a 10-fold increase in bulk modulus.
Roy
Rani
R
Department of Biomedical Engineering, 149 Weill Hall, Cornell University, Ithaca, New York 14853, USA.
Boskey
Adele
A
Bonassar
Lawrence J
LJ
D000818:Animals; D024042:Collagen Type I / Q000378:metabolism*; D004548:Elasticity / Q000187:drug effects; D004798:Enzymes / Q000378:metabolism; D005453:Fluorescence; D005782:Gels / Q000378:metabolism*; D006031:Glycosylation / Q000187:drug effects; D051381:Rats; D012266:Ribose / Q000494:pharmacology; D017550:Spectroscopy, Fourier Transform Infrared; D014783:Viscosity / Q000187:drug effects
D024042:Collagen Type I; D004798:Enzymes; D005782:Gels; D012266:Ribose