title: Dimerization effects on coacervation property of an elastin-derived synthetic peptide (FPGVG)5.
abstract: Elastin, a core protein of the elastic fibers, exhibits the coacervation (temperature-dependent reversible association/dissociation) under physiological conditions. Because of this characteristic, elastin and elastin-derived peptides have been considered to be useful as base materials for developing various biomedical products, skin substitutes, synthetic vascular grafts, and drug delivery systems. Although elastin-derived polypeptide (Val-Pro-Gly-Val-Gly)n also has been known to demonstrate coacervation property, a sufficiently high (VPGVG)n repetition number (n>40) is required for coacervation. In the present study, a series of elastin-derived peptide (Phe-Pro-Gly-Val-Gly)5 dimers possessing high coacervation potential were newly developed. These novel dimeric peptides exhibited coacervation at significantly lower concentrations and temperatures than the commonly used elastin-derived peptide analogs; this result suggests that the coacervation ability of the peptides is enhanced by dimerization. Circular dichroism (CD) measurements indicate that the dimers undergo similar temperature-dependent and reversible conformational changes when coacervation occurs. The molecular dynamics calculation results reveal that the sheet-turn-sheet motif involving a type II β-turn-like structure commonly observed among the dimers and caused formation of globular conformation of them. These synthesized peptide dimers may be useful not only as model peptides for structural analysis of elastin and elastin-derived peptides, but also as base materials for developing various temperature-sensitive biomedical and industrial products.
authors.affiliation: Faculty of Arts and Science, Kyushu University, Fukuoka, 819-0395, Japan.
authors.forename: Keitaro
authors.initials: K
authors.lastname: Suyama
authors.affiliation: Department of Bioscience and Bioinformatics, Graduate School of Computer Science and Systems Engineering, Kyushu Institute of Technology, Iizuka, Fukuoka, 820-8502, Japan.
authors.forename: Suguru
authors.initials: S
authors.lastname: Taniguchi
authors.affiliation: Department of Chemistry, Faculty and Graduate School of Science, Kyushu University, Fukuoka, 819-0395, Japan.
authors.forename: Daiki
authors.initials: D
authors.lastname: Tatsubo
authors.affiliation: Department of Bioscience and Bioinformatics, Graduate School of Computer Science and Systems Engineering, Kyushu Institute of Technology, Iizuka, Fukuoka, 820-8502, Japan.
authors.forename: Iori
authors.initials: I
authors.lastname: Maeda
authors.affiliation: Faculty of Arts and Science, Kyushu University, Fukuoka, 819-0395, Japan.|Department of Chemistry, Faculty and Graduate School of Science, Kyushu University, Fukuoka, 819-0395, Japan.
authors.forename: Takeru
authors.initials: T
authors.lastname: Nose
mesh_terms: D000595:Amino Acid Sequence; D004549:Elastin / Q000737:chemistry*; D006860:Hydrogen Bonding; D056004:Molecular Dynamics Simulation; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation; D055503:Protein Multimerization
chemical_list: D009842:Oligopeptides; D004549:Elastin
keywords: circular dichroism (CD) measurements; coacervation; dimerization; elastin-derived peptide; molecular dynamics calculation