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In vivo effects of tailored laminin‐332 α3 conjugated scaffolds enhances wound healing: A histomorphometric analysis
Author(s) -
Damodaran Gopinath,
Tiong William H. C.,
Collighan Russell,
Griffin Martin,
Navsaria Harshad,
Pandit Abhay
Publication year - 2013
Publication title -
journal of biomedical materials research part a
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.849
H-Index - 150
eISSN - 1552-4965
pISSN - 1549-3296
DOI - 10.1002/jbm.a.34583
Subject(s) - wound healing , laminin , tissue transglutaminase , cell adhesion , peptide , angiogenesis , materials science , neovascularization , tissue engineering , fibroblast , adhesion , microbiology and biotechnology , biomedical engineering , extracellular matrix , chemistry , biochemistry , in vitro , cancer research , biology , medicine , immunology , enzyme , composite material
Surface modification techniques have been used to develop biomimetic scaffolds by incorporating cell adhesion peptides. In our previous work, we have shown the tethering of laminin‐332 α3 chain to type I collagen scaffold using microbial transglutaminase (mTGase), promotes cell adhesion, migration, and proliferation. In this study, we evaluated the wound healing properties of tailored laminin‐332 α3 chain (peptide A: PPFLMLLKGSTR) tethered to a type I collagen scaffold using mTGase by incorporating transglutaminase substrate peptide sequences containing either glutamine (peptide B: PPFLMLLKGSTR EAQQIVM ) or lysine (peptide C: PPFLMLLKGSTR KKKKG ) in rat full‐thickness wound model at two different time points (7 and 21 days). Histological evaluations were assessed for wound closure, epithelialization, angiogenesis, inflammatory, fibroblastic cellular infiltrations, and quantified using stereological methods ( p < 0.05). Peptide A and B tethered to collagen scaffold using mTGase stimulated neovascularization, decreased the inflammatory cell infiltration and prominently enhanced the fibroblast proliferation which significantly accelerated the wound healing process. We conclude that surface modification by incorporating motif of laminin‐332 α3 chain (peptide A: PPFLMLLK GSTR) domain and transglutaminase substrate to the laminin‐332 α3 chain (peptide B: PPFLMLLKGSTR EAQQIVM ) using mTGase may be a potential candidate for tissue engineering applications and skin regeneration. © 2013 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 101A:2788–2795, 2013.