Structural requirements essential for elastin coacervation: favorable spatial arrangements of valine ridges on the three-dimensional structure of elastin-derived polypeptide (VPGVG)n.
J Pept Sci
; 17(11): 735-43, 2011 Nov.
Article
em En
| MEDLINE
| ID: mdl-21919131
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 (1) H-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 ß-spiral structure required for self-association followed by coacervation, probably due to the ideal spatial arrangement of the hydrophobic Val residues.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Elastina
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
J Pept Sci
Assunto da revista:
BIOQUIMICA
Ano de publicação:
2011
Tipo de documento:
Article
País de afiliação:
Japão