Influence of telopeptides, fibrils and crosslinking on physicochemical properties of Type i collagen films

Robin S. Walton, David Brand, Jan T. Czernuszka

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

Type I collagen is widely used in various different forms for research and commercial applications. Different forms of collagen may be classified according to their source, extraction method, crosslinking and resultant ultrastructure. In this study, afibrillar and reconstituted fibrillar films, derived from acid soluble and pepsin digested Type I collagen, were analysed using Lateral Force Microscopy (LFM), Fourier Transform Infra-Red Spectroscopy (FTIR), Differential Scanning Calorimetry (DSC) and enzymatic stability assays to asses the influence of telopeptides, fibrils and crosslinking. LFM proved to be a useful technique to confirm an afibrillar/fibrillar ultrastructure and to elucidate fibril diameters. FTIR has proved insensitive to ultrastructural differences involving telopeptides and fibrils. DSC results showed a significant increase in T d for crosslinked samples (+22-28°C), and demonstrated that the thermal behaviour of hydrated, afibrillar films is more akin to reconstituted fibrillar films than monomeric solutions. The enzymatic stability assay has provided new evidence to show that afibrillar films of Type I collagen can be significantly more resistant to collagenase (by up to 3.5 times), than reconstituted fibrillar films, as a direct consequence of the different spatial arrangement of collagen molecules. A novel mechanism for this phenomenon is proposed and discussed. Additionally, the presence of telopeptide regions in afibrillar tropocollagen samples has been shown to increase resistance to collagenase by greater than 3.5 times compared to counterpart afibrillar atelocollagen samples. One-factor ANOVA analysis, with Fisher's LSD post-hoc test, confirms these key findings to be of statistical significance (P < 0.05). The profound physicochemical effects of collagen ultrastructure demonstrated in this study reiterates the need for comprehensive materials disclosure and classification when using these biomaterials.

Original languageEnglish (US)
Pages (from-to)451-461
Number of pages11
JournalJournal of Materials Science: Materials in Medicine
Volume21
Issue number2
DOIs
StatePublished - Feb 1 2010
Externally publishedYes

Fingerprint

crosslinking
collagens
Collagen Type I
Collagen
Crosslinking
Atomic Force Microscopy
Differential Scanning Calorimetry
Enzyme Assays
Collagenases
Fourier Analysis
Spectrum Analysis
Tropocollagen
Lysergic Acid Diethylamide
Equidae
Pepsin A
Disclosure
Biocompatible Materials
Differential scanning calorimetry
Infrared spectroscopy
Assays

All Science Journal Classification (ASJC) codes

  • Bioengineering
  • Biophysics
  • Biomaterials
  • Biomedical Engineering

Cite this

Influence of telopeptides, fibrils and crosslinking on physicochemical properties of Type i collagen films. / Walton, Robin S.; Brand, David; Czernuszka, Jan T.

In: Journal of Materials Science: Materials in Medicine, Vol. 21, No. 2, 01.02.2010, p. 451-461.

Research output: Contribution to journalArticle

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