title: Amino acid sequence preferences to control cell-specific organization of endothelial cells, smooth muscle cells, and fibroblasts.
abstract: Effective surface modification with biocompatible molecules is known to be effective in reducing the life-threatening risks related to artificial cardiovascular implants. In recent strategies in regenerative medicine, the enhancement and support of natural repair systems at the site of injury by designed biocompatible molecules have succeeded in rapid and effective injury repair. Therefore, such a strategy could also be effective for rapid endothelialization of cardiovascular implants to lower the risk of thrombosis and stenosis. To achieve this enhancement of the natural repair system, a biomimetic molecule that mimics proper cellular organization at the implant location is required. In spite of the fact that many reported peptides have cell-attracting properties on material surfaces, there have been few peptides that could control cell-specific adhesion. For the advanced cardiovascular implants, peptides that can mimic the natural mechanism that controls cell-specific organization have been strongly anticipated. To obtain such peptides, we hypothesized the cellular bias toward certain varieties of amino acids and examined the cell preference (in terms of adhesion, proliferation, and protein attraction) of varieties and of repeat length on SPOT peptide arrays. To investigate the role of specific peptides in controlling the organization of various cardiovascular-related cells, we compared endothelial cells (ECs), smooth muscle cells (SMCs), and fibroblasts (FBs). A clear, cell-specific preference was found for amino acids (longer than 5-mer) using three types of cells, and the combinational effect of the physicochemical properties of the residues was analyzed to interpret the mechanism.
authors.affiliation: Department of Biotechnology, Graduate School of Engineering, Nagoya University, Nagoya, Aichi, Japan.
authors.forename: Kei
authors.initials: K
authors.lastname: Kanie
authors.forename: Ryuji
authors.initials: R
authors.lastname: Kato
authors.forename: Yingzi
authors.initials: Y
authors.lastname: Zhao
authors.forename: Yuji
authors.initials: Y
authors.lastname: Narita
authors.forename: Mina
authors.initials: M
authors.lastname: Okochi
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Honda
mesh_terms: D000595:Amino Acid Sequence; D001798:Blood Proteins / Q000378:metabolism; D002448:Cell Adhesion / Q000187:drug effects; D049109:Cell Proliferation / Q000187:drug effects; D042783:Endothelial Cells / Q000187:drug effects* / Q000378:metabolism / Q000648:ultrastructure; D016326:Extracellular Matrix Proteins / Q000378:metabolism; D005347:Fibroblasts / Q000187:drug effects* / Q000378:metabolism / Q000648:ultrastructure; D006801:Humans; D066298:In Vitro Techniques; D032389:Myocytes, Smooth Muscle / Q000187:drug effects* / Q000378:metabolism / Q000648:ultrastructure; D009842:Oligopeptides / Q000737:chemistry* / Q000494:pharmacology; D019151:Peptide Library; D040081:Protein Array Analysis; D011485:Protein Binding; D013329:Structure-Activity Relationship
chemical_list: D001798:Blood Proteins; D016326:Extracellular Matrix Proteins; D009842:Oligopeptides; D019151:Peptide Library