Tethering a laminin peptide to a crosslinked collagen scaffold for biofunctionality

Gopinath Damodaran, Russell Collighan, Martin Griffin, Abhay Pandit

Research output: Contribution to journalArticle

Abstract

Cell adhesion peptide regulates various cellular functions like proliferation, attachment, and spreading. The cellular response to laminin peptide (PPFLMLLKGSTR), a motif of laminin-5 alpha3 chain, tethered to type I collagen, crosslinked using microbial transglutaminase (mTGase) was investigated. mTGase is an enzyme that initiates crosslinking by reacting with the glutamine and lysine residues on the collagen fibers stabilizing the molecular structure. In this study that tethering of the laminin peptide in a mTGase crosslinked collagen scaffold enhanced cell proliferation and attachment. Laminin peptide tethered crosslinked scaffold showed unaltered cell morphology of 3T3 fibroblasts when compared with collagen and crosslinked scaffold. The triple helical structure of collagen remained unaltered by the addition of laminin peptide. In addition a dose-dependent affinity of the laminin peptide towards collagen was seen. The degree of crosslinking was measured by amino acid analysis, differential scanning calorimeter and fourier transform infrared spectroscopy. Increased crosslinking was observed in mTGase crosslinked group. mTGase crosslinking showed higher shrinkage temperature. There was alteration in the fibrillar architecture due to the crosslinking activity of mTGase. Hence, the use of enzyme-mediated linking shows promise in tethering cell adhesive peptides through biodegradable scaffolds.
LanguageEnglish
Pages1001-1010
Number of pages10
JournalJournal of Biomedical Materials Research: Part A
Volume89A
Issue number4
DOIs
Publication statusPublished - 15 Jun 2009

Fingerprint

Laminin
Scaffolds (biology)
Transglutaminases
Collagen
Peptides
Crosslinking
Scaffolds
Enzymes
Cell adhesion
Cell proliferation
Fibroblasts
Collagen Type I
Glutamine
Calorimeters
Molecular structure
Lysine
Fourier transform infrared spectroscopy
Amino acids
Adhesives
Scanning

Keywords

  • collagen
  • laminin peptide
  • microbial transglutaminase

Cite this

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title = "Tethering a laminin peptide to a crosslinked collagen scaffold for biofunctionality",
abstract = "Cell adhesion peptide regulates various cellular functions like proliferation, attachment, and spreading. The cellular response to laminin peptide (PPFLMLLKGSTR), a motif of laminin-5 alpha3 chain, tethered to type I collagen, crosslinked using microbial transglutaminase (mTGase) was investigated. mTGase is an enzyme that initiates crosslinking by reacting with the glutamine and lysine residues on the collagen fibers stabilizing the molecular structure. In this study that tethering of the laminin peptide in a mTGase crosslinked collagen scaffold enhanced cell proliferation and attachment. Laminin peptide tethered crosslinked scaffold showed unaltered cell morphology of 3T3 fibroblasts when compared with collagen and crosslinked scaffold. The triple helical structure of collagen remained unaltered by the addition of laminin peptide. In addition a dose-dependent affinity of the laminin peptide towards collagen was seen. The degree of crosslinking was measured by amino acid analysis, differential scanning calorimeter and fourier transform infrared spectroscopy. Increased crosslinking was observed in mTGase crosslinked group. mTGase crosslinking showed higher shrinkage temperature. There was alteration in the fibrillar architecture due to the crosslinking activity of mTGase. Hence, the use of enzyme-mediated linking shows promise in tethering cell adhesive peptides through biodegradable scaffolds.",
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Tethering a laminin peptide to a crosslinked collagen scaffold for biofunctionality. / Damodaran, Gopinath; Collighan, Russell; Griffin, Martin; Pandit, Abhay.

In: Journal of Biomedical Materials Research: Part A, Vol. 89A, No. 4, 15.06.2009, p. 1001-1010.

Research output: Contribution to journalArticle

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