What is it about?
The new dimeric elastin-derived peptide showed significantly high coacervation ability compared to known elastin-derived peptide analogs. The MD calculation results reveal that the dimeric peptides contain characteristic sheet-turn-sheet motif involving a type II β-turn-like structure and form globular conformation.
Featured Image
Why is it important?
The simple dimerization of the elastin-derived peptide, (FPGVG)n, analogs significantly enhanced its coacervation ability.
Perspectives
Such forced dimerization techniques will enable the creation of new functional biomaterials and molecular devices that combine both the properties of coacervation and new functions in a single molecule.
Prof Takeru Nose
Kyushu Daigaku
Read the Original
This page is a summary of: Dimerization effects on coacervation property of an elastin-derived synthetic peptide (FPGVG)5, Journal of Peptide Science, March 2016, Wiley,
DOI: 10.1002/psc.2876.
You can read the full text:
Contributors
The following have contributed to this page
