76911-65-4Relevant academic research and scientific papers
Sequential Polypeptides of Elastin: Cyclic Conformational Correlates of the Linear Polypentapeptide
Urry, Dan W.,Trapane, Tina L.,Sugano, Hiroshi,Prasad, Kari U.
, p. 2080 - 2089 (1981)
Cyclic oligomers of the repeating pentamer sequence of the elastic fiber, (Val1-Pro2,Gly3-Val4-Gly5)n, were synthesized with n = 1-6, and the cyclic oligomers were studied by means of proto
Temperature-sensitive elastin-mimetic dendrimers: Effect of peptide length and dendrimer generation to temperature sensitivity
Kojima, Chie,Irie, Kotaro,Tada, Tomoko,Tanaka, Naoki
, p. 603 - 612 (2014/04/17)
Dendrimers are synthetic macromolecules with unique structure, which are a potential scaffold for peptides. Elastin is one of the main components of extracellular matrix and a temperature-sensitive biomacromolecule. Previously, Val-Pro-Gly-Val-Gly peptides have been conjugated to a dendrimer for designing an elastin-mimetic dendrimer. In this study, various elastin-mimetic dendrimers using different length peptides and different dendrimer generations were synthesized to control the temperature dependency. The elastin-mimetic dendrimers formed β-turn structure by heating, which was similar to the elastin-like peptides. The elastin-mimetic dendrimers exhibited an inverse phase transition, largely depending on the peptide length and slightly depending on the dendrimer generation. The elastin-mimetic dendrimers formed aggregates after the phase transition. The endothermal peak was observed in elastin-mimetic dendrimers with long peptides, but not with short ones. The peptide length and the dendrimer generation are important factors to tune the temperature dependency on the elastin-mimetic dendrimer. Copyright
