title: Proliferative activity of elastin-like-peptides depends on charge and phase transition.
abstract: Elastin-like-peptides (ELPs) are stimulus-responsive protein-based polymers and are attractive biomaterials due to their biocompatibility and unique properties. This study shows that in addition to their physical properties, ELPs have biological activities that are conducive to tissue regeneration. Specifically, we found that ELPs induce fibroblast proliferation via cell surface heparan sulfate proteoglycans (HSPG). Furthermore, our data suggests that ELP based materials with differential proliferative potential can be designed by controlling the interaction of ELPs with HSPGs by incorporating either hydrophobic or positively charged residues within the ELP sequence. Fibroblast proliferation is important for granulation tissue formation which is important in chronic wounds as well as in healing of other tissues. The customizable biological activity of ELPs coupled with their unique physical properties will enable us to design novel, sustainable and cost effective therapies for different tissue regeneration applications. © 2015 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 104A: 697-706, 2016.
authors.affiliation: Department of Chemical and Biomedical Engineering, University of South Florida, Tampa, Florida, 33620.
authors.forename: Yuan
authors.initials: Y
authors.lastname: Yuan
authors.affiliation: Department of Chemical and Biomedical Engineering, University of South Florida, Tampa, Florida, 33620.
authors.forename: Piyush
authors.initials: P
authors.lastname: Koria
mesh_terms: D000595:Amino Acid Sequence; D002460:Cell Line; D049109:Cell Proliferation / Q000187:drug effects; D003432:Cross-Linking Reagents / Q000494:pharmacology; D004549:Elastin / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D005347:Fibroblasts / Q000166:cytology / Q000187:drug effects / Q000201:enzymology; D015971:Gene Expression Regulation, Enzymologic / Q000187:drug effects; D019812:Heparan Sulfate Proteoglycans / Q000378:metabolism; D006801:Humans; D055767:Immobilized Proteins / Q000494:pharmacology; D020782:Matrix Metalloproteinases / Q000235:genetics / Q000378:metabolism; D008934:Mitogens / Q000494:pharmacology; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D044367:Phase Transition; D011956:Receptors, Cell Surface / Q000378:metabolism; D012867:Skin / Q000166:cytology; D013696:Temperature
chemical_list: D003432:Cross-Linking Reagents; D019812:Heparan Sulfate Proteoglycans; D055767:Immobilized Proteins; D008934:Mitogens; D010455:Peptides; D011956:Receptors, Cell Surface; C054901:elastin-binding proteins; D004549:Elastin; D020782:Matrix Metalloproteinases
keywords: elastin-like peptides; fibroblast proliferation; tissue regeneration