Structural requirements essential for elastin coacervation

Favorable spatial arrangements of valine ridges on the three-dimensional structure of elastin-derived polypeptide (VPGVG)n

Iori Maeda, Yoshiteru Fukumoto, Takeru Nose, Yasuyuki Shimohigashi, Takashi Nezu, Yoshihiro Terada, Hiroaki Kodama, Kozue Kaibara, Kouji Okamoto

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

The elastin precursor tropoelastin possesses a number of polymeric peptides with repeating 3-9 mer sequences. One of these is the pentapeptide Val-Pro-Gly-Val-Gly (VPGVG) present in almost all animal species, and its polymer (VPGVG)n coacervates just as does tropoelastin. In the present study, in order to explore the structural requirements essential for coacervation, (VPGVG)n and its shortened repeat analogs (VPGV)n, (VPG)n, and (PGVG)n were synthesized and their structural properties were investigated. In our turbidity measurements, (VPGVG)n demonstrated complete reversible coacervation in agreement with previous findings. The Gly 5-deleted polymer (VPGV)n also achieved self-association, though the onset of self-association occurred at a lower temperature. However, the dissociation of (VPGV)n upon temperature lowering was found to occur in a three-step process; the Val i 4-Val i+1 1 structure arising in the VPGV polypeptide appeared to perturb the dissociation. No self-association was observed for (VPG)n or (PGVG)n repeats. Spectroscopic measurements by CD, FT-IR, and 1H-NMR showed that the (VPGV)n and (VPG)n both assumed ordered structures similar to that of (VPGVG)n. These results demonstrated that VPGVG is a structural element essential to achieving the β-spiral structure required for self-association followed by coacervation, probably due to the ideal spatial arrangement of the hydrophobic Val residues.

Original languageEnglish
Pages (from-to)735-743
Number of pages9
JournalJournal of Peptide Science
Volume17
Issue number11
DOIs
Publication statusPublished - Nov 1 2011

Fingerprint

valyl-prolyl-glycyl-valyl-glycine
Elastin
Valine
Tropoelastin
Association reactions
Peptides
Polymers
Turbidity
Structural properties
Animals
Temperature
Nuclear magnetic resonance

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Organic Chemistry

Cite this

Structural requirements essential for elastin coacervation : Favorable spatial arrangements of valine ridges on the three-dimensional structure of elastin-derived polypeptide (VPGVG)n. / Maeda, Iori; Fukumoto, Yoshiteru; Nose, Takeru; Shimohigashi, Yasuyuki; Nezu, Takashi; Terada, Yoshihiro; Kodama, Hiroaki; Kaibara, Kozue; Okamoto, Kouji.

In: Journal of Peptide Science, Vol. 17, No. 11, 01.11.2011, p. 735-743.

Research output: Contribution to journalArticle

Maeda, Iori ; Fukumoto, Yoshiteru ; Nose, Takeru ; Shimohigashi, Yasuyuki ; Nezu, Takashi ; Terada, Yoshihiro ; Kodama, Hiroaki ; Kaibara, Kozue ; Okamoto, Kouji. / Structural requirements essential for elastin coacervation : Favorable spatial arrangements of valine ridges on the three-dimensional structure of elastin-derived polypeptide (VPGVG)n. In: Journal of Peptide Science. 2011 ; Vol. 17, No. 11. pp. 735-743.
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AU - Nezu, Takashi

AU - Terada, Yoshihiro

AU - Kodama, Hiroaki

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AU - Okamoto, Kouji

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AB - The elastin precursor tropoelastin possesses a number of polymeric peptides with repeating 3-9 mer sequences. One of these is the pentapeptide Val-Pro-Gly-Val-Gly (VPGVG) present in almost all animal species, and its polymer (VPGVG)n coacervates just as does tropoelastin. In the present study, in order to explore the structural requirements essential for coacervation, (VPGVG)n and its shortened repeat analogs (VPGV)n, (VPG)n, and (PGVG)n were synthesized and their structural properties were investigated. In our turbidity measurements, (VPGVG)n demonstrated complete reversible coacervation in agreement with previous findings. The Gly 5-deleted polymer (VPGV)n also achieved self-association, though the onset of self-association occurred at a lower temperature. However, the dissociation of (VPGV)n upon temperature lowering was found to occur in a three-step process; the Val i 4-Val i+1 1 structure arising in the VPGV polypeptide appeared to perturb the dissociation. No self-association was observed for (VPG)n or (PGVG)n repeats. Spectroscopic measurements by CD, FT-IR, and 1H-NMR showed that the (VPGV)n and (VPG)n both assumed ordered structures similar to that of (VPGVG)n. These results demonstrated that VPGVG is a structural element essential to achieving the β-spiral structure required for self-association followed by coacervation, probably due to the ideal spatial arrangement of the hydrophobic Val residues.

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