title: Comparison between coacervation property and secondary structure of synthetic peptides, Ile-containing elastin-derived pentapeptide repeats.
abstract: A series of Ile-containing elastin-derived peptide-analogs, (Ile-Pro-Gly-Val-Gly)n (n = 7-10) possessing remarkable and reversible coacervation property were newly synthesized. In comparison with the known elastin-derived peptide-analogs, which were so-called polypeptides, the obtained 35 to 50 mer peptides, (IPGVG)n (n = 7-10) were significantly low molecular sized-polypeptides. However, they clearly exhibited coacervation property as same as the polypeptides did. Because of their low molecular size, spectrographic analyses of (IPGVG)n (n = 7-10) became feasible to carry out. As results of secondary structural analyses by CD and FT-IR, it was found that the coacervation property of the peptides is clearly attributed to the ordered secondary-structures, mainly, type II β-turn.
authors: Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Iizuka, Fukuoka 820-8502, Japan. iori@kyutech.ac.jp
authors: Iori
authors: I
authors: Maeda
authors: Suguru
authors: S
authors: Taniguchi
authors: Junko
authors: J
authors: Ebina
authors: Noriko
authors: N
authors: Watanabe
authors: Takao
authors: T
authors: Hattori
authors: Takeru
authors: T
authors: Nose
mesh_terms: D004549:Elastin / Q000737:chemistry*; D007532:Isoleucine / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary
chemical_list: D010455:Peptides; D007532:Isoleucine; D004549:Elastin