Literature DB >> 30449450

Matrikines for therapeutic and biomedical applications.

K Sivaraman1, C Shanthi2.   

Abstract

Matrikines, peptides originating from the fragmentation of extracellular matrix proteins are identified to play important role in both health and disease. They possess biological activities, much different from their parent protein. Identification of such bioactive cryptic regions in the extracellular matrix proteins has attracted the researchers all over the world in the recent decade. These bioactive peptides could find use in preparation of biomaterials and tissue engineering applications. Matrikines identified in major extracellular matrix (ECM) proteins like collagen, elastin, fibronectin, and laminin are being extensively studied for use in tissue engineering and regenerative medicine. They are identified to modulate cellular activity like cell growth, proliferation, migration and may induce apoptosis. RGD, a well-known peptide identified in fibronectin with cell adhesive property is being investigated in designing biomaterials. Collagen hexapeptide GFOGER was found to promote cell adhesion and differentiation. Laminin also possesses regions with strong cell adhesion property. Recently, cell-penetrating peptides from elastin are used as a targeted delivery system for therapeutic drugs. The continued search for cryptic sequences in the extracellular matrix proteins along with advanced peptide coupling chemistries would lead to biomaterials with improved surface properties. This review article outlines the peptides derived from extracellular matrix and some of the possible applications of these peptides in therapeutics and tissue engineering applications.
Copyright © 2018 Elsevier Inc. All rights reserved.

Entities:  

Keywords:  Biomedical; ECM; Matrikines; Peptides; Therapeutics; Tissue engineering

Mesh:

Substances:

Year:  2018        PMID: 30449450     DOI: 10.1016/j.lfs.2018.10.056

Source DB:  PubMed          Journal:  Life Sci        ISSN: 0024-3205            Impact factor:   5.037


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