Comparison between coacervation property and secondary structure of synthetic peptides, ile-containing elastin-derived pentapeptide repeats

Iori Maeda; Suguru Taniguchi; Junko Ebina; Noriko Watanabe; Takao Hattori; Takeru Nose

doi:10.2174/0929866511320080007

Comparison between coacervation property and secondary structure of synthetic peptides, ile-containing elastin-derived pentapeptide repeats

Iori Maeda, Suguru Taniguchi, Junko Ebina, Noriko Watanabe, Takao Hattori, Takeru Nose

Division for Experimental Natural Science

Research output: Contribution to journal › Article › peer-review

13 Citations (Scopus)

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 peptideanalogs, 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.

Original language	English
Pages (from-to)	905-910
Number of pages	6
Journal	Protein and Peptide Letters
Volume	20
Issue number	8
DOIs	https://doi.org/10.2174/0929866511320080007
Publication status	Published - Aug 2013

All Science Journal Classification (ASJC) codes

Structural Biology
Biochemistry

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10.2174/0929866511320080007

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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 peptideanalogs, 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.",

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T1 - Comparison between coacervation property and secondary structure of synthetic peptides, ile-containing elastin-derived pentapeptide repeats

AU - Maeda, Iori

AU - Taniguchi, Suguru

AU - Ebina, Junko

AU - Watanabe, Noriko

AU - Hattori, Takao

AU - Nose, Takeru

PY - 2013/8

Y1 - 2013/8

N2 - 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 peptideanalogs, 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.

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Comparison between coacervation property and secondary structure of synthetic peptides, ile-containing elastin-derived pentapeptide repeats

Abstract

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