Structure and dynamics of water in native and tanned collagen fibers: Effect of crosslinking.
The influence of crosslinking on the hydration structure of collagen has been investigated. Nuclear magnetic resonance, dielectric relaxation and thermoporometry were used to investigate water structure in native and crosslinked collagen fibers on both wet and dried specimen. Measurements reveal the influence of different chemical treatments on the transverse relaxation time and polarization of the collagen fibers. The frequency dependence of dielectric constant of collagen fibers displays an induction behavior on low frequencies. Bound water constrained in collagen fibers seems to provide signatures for changes induced by crosslinking agents on the pore diameter and distribution in collagen fibers. A correlation of transverse relaxation time of water in dry and wet states presented in this study presents an experimental tool for examining the differences in efficacy of crosslinking agents. Changes in the dielectric relaxation, dynamics of water structure and hydroporometric structure of collagen are dependent on the nature of crosslinking material.
Fathima
N Nishad
NN
Chemical Laboratory, Central Leather Research Institute, Council of Scientific and Industrial Research, Adyar, Chennai, India.
Baias
M
M
Blumich
B
B
Ramasami
T
T
D000818:Animals; D003432:Cross-Linking Reagents / Q000737:chemistry*; D004560:Electricity; D024022:Fibrillar Collagens / Q000737:chemistry*; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D016062:Porosity; D051381:Rats; D013696:Temperature; D014867:Water / Q000737:chemistry*
D003432:Cross-Linking Reagents; D024022:Fibrillar Collagens; D008024:Ligands; D014867:Water