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 language | English |
|---|---|
| Pages (from-to) | 735-743 |
| Number of pages | 9 |
| Journal | Journal of Peptide Science |
| Volume | 17 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - Nov 1 2011 |
Fingerprint
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 journal › Article
}
TY - JOUR
T1 - Structural requirements essential for elastin coacervation
T2 - Favorable spatial arrangements of valine ridges on the three-dimensional structure of elastin-derived polypeptide (VPGVG)n
AU - Maeda, Iori
AU - Fukumoto, Yoshiteru
AU - Nose, Takeru
AU - Shimohigashi, Yasuyuki
AU - Nezu, Takashi
AU - Terada, Yoshihiro
AU - Kodama, Hiroaki
AU - Kaibara, Kozue
AU - Okamoto, Kouji
PY - 2011/11/1
Y1 - 2011/11/1
N2 - 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.
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.
UR - http://www.scopus.com/inward/record.url?scp=80055006040&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=80055006040&partnerID=8YFLogxK
U2 - 10.1002/psc.1394
DO - 10.1002/psc.1394
M3 - Article
VL - 17
SP - 735
EP - 743
JO - Journal of Peptide Science
JF - Journal of Peptide Science
SN - 1075-2617
IS - 11
ER -