Structure and dynamics of water in native and tanned collagen fibers: Effect of crosslinking

N. Nishad Fathima, Maria Baias, B. Blumich, T. Ramasami

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)590-596
Number of pages7
JournalInternational Journal of Biological Macromolecules
Volume47
Issue number5
DOIs
StatePublished - Dec 1 2010

Fingerprint

Crosslinking
Collagen
Water
Fibers
Dielectric relaxation
Relaxation time
Hydration
Permittivity
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
Polarization

Keywords

  • Collagen
  • Crosslinking
  • Dielectric spectroscopy
  • Hydration
  • Nuclear magnetic resonance (NMR)
  • Thermoporometry

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

Cite this

Structure and dynamics of water in native and tanned collagen fibers : Effect of crosslinking. / Fathima, N. Nishad; Baias, Maria; Blumich, B.; Ramasami, T.

In: International Journal of Biological Macromolecules, Vol. 47, No. 5, 01.12.2010, p. 590-596.

Research output: Contribution to journalArticle

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