Enhancement of self-aggregation properties of linear elastin-derived short peptides by simple cyclization: strong self-aggregation properties of cyclo[FPGVG]n, consisting only of natural amino acids

Keitaro Suyama, Daiki Tatsubo, Wataru Iwasaki, Masaya Miyazaki, Yuhei Kiyota, Ichiro Takahashi, Iori Maeda, Takeru Nose

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Elastin-like peptides (ELP) consist of distinctive repetitive sequences, such as (VPGVG)n, exhibit temperature-dependent reversible self-assembly (coacervation), and have been considered to be useful for the development of thermo-responsive materials. Further fundamental studies evaluating coacervative properties of novel nonlinear ELPs could present design concepts for new thermo-responsive materials. In this study, we prepared novel ELPs, cyclic (FPGVG)n (cyclo[FPGVG]n, n = 1-5), and analyzed its self-assembly properties and structural characteristics. Cyclo[FPGVG]n (n = 3-5) demonstrated stronger coacervation capacity than the corresponding linear peptides. The coacervate of cyclo[FPGVG]5 was able to retain water-soluble dye molecules at 40°C, which implied that cyclo[FPGVG]5 could be employed as a base material of DDS (Drug Delivery System) matrices and other biomaterials. The results of molecular dynamics simulations and circular dichroism measurements suggested that a certain chain length was required for cyclo[FPGVG]n to demonstrate alterations in molecular structure that were critical to the exhibition of coacervation.

Original languageEnglish
Pages (from-to)3201-3211
Number of pages11
JournalBiomacromolecules
Volume19
Issue number8
DOIs
Publication statusPublished - Jun 22 2018

Fingerprint

Elastin
Cyclization
Peptides
Amino acids
Agglomeration
valyl-prolyl-glycyl-valyl-glycine
Amino Acids
Self assembly
Nucleic Acid Repetitive Sequences
Dichroism
Biocompatible Materials
Chain length
Biomaterials
Molecular structure
Molecular dynamics
Coloring Agents
Dyes
Molecules
Water
Computer simulation

All Science Journal Classification (ASJC) codes

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

Cite this

Enhancement of self-aggregation properties of linear elastin-derived short peptides by simple cyclization : strong self-aggregation properties of cyclo[FPGVG]n, consisting only of natural amino acids. / Suyama, Keitaro; Tatsubo, Daiki; Iwasaki, Wataru; Miyazaki, Masaya; Kiyota, Yuhei; Takahashi, Ichiro; Maeda, Iori; Nose, Takeru.

In: Biomacromolecules, Vol. 19, No. 8, 22.06.2018, p. 3201-3211.

Research output: Contribution to journalArticle

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