CaltechAUTHORS
  A Caltech Library Service

Mechanism for the Phase Transition of a Genetically Engineered Elastin Model Peptide (VPGIG)_(40) in Aqueous Solution

Yamaoka, Tetsuji and Tamura, Takumi and Seto, Yuuki and Tada, Tomoko and Kunugi, Shigeru and Tirrell, David A. (2003) Mechanism for the Phase Transition of a Genetically Engineered Elastin Model Peptide (VPGIG)_(40) in Aqueous Solution. Biomacromolecules, 4 (6). pp. 1680-1685. ISSN 1525-7797. doi:10.1021/bm034120l. https://resolver.caltech.edu/CaltechAUTHORS:20150109-113118565

Full text is not posted in this repository. Consult Related URLs below.

Use this Persistent URL to link to this item: https://resolver.caltech.edu/CaltechAUTHORS:20150109-113118565

Abstract

The concentration dependence of the pressure- and temperature-induced cloud point transition (P_c and T_c, respectively) of aqueous solutions of an elastin-like polypeptide with a repeating pentapeptide Val−Pro−Gly−Ile−Gly sequence (MGLDGSMG(VPGIG)_(40)VPLE) was investigated by using apparent light scattering, differential scanning calorimetry, and circular dichroism methods. In addition, the effects of salts and surfactants on these properties were investigated. The P_c and T_c of the present peptide in aqueous solution were strongly concentration dependent. The calorimetric measurements showed that the enthalpy of transitions was 300−400 kJ/mol, i.e., 7−10 kJ/mol per VPGIG pentamer. The T_c of the (VPGIG)_(40) solution was highly affected by the addition of inert salts or SDS. The effects of salts were consistent with those observed in the lyotropic series or Hoffmeister series. The CD spectrum at low peptide concentrations indicated that the present peptide forms type II β-turn-like structure(s) at higher temperatures, but the temperature dependence of random coil diminishment (195 nm) and β-turn formation (210 nm) were not exactly coincident. A hypothetical mechanism of the (VPGIG)_(40) phase transition that could account for these observations was postulated. Observations suggest that the temperature-responsive properties of the elastin model peptides occur via a mechanism involving conformational change−association−aggregation and that the first two are strongly interactive.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1021/bm034120lDOIArticle
http://pubs.acs.org/doi/abs/10.1021/bm034120lPublisherArticle
ORCID:
AuthorORCID
Tirrell, David A.0000-0003-3175-4596
Alternate Title:Mechanism for the Phase Transition of a Genetically Engineered Elastin Model Peptide (VPGIG)40 in Aqueous Solution
Additional Information:© 2003 American Chemical Society. Published In Issue November 10, 2003. Publication Date (Web): September 5, 2003. Received April 19, 2003. Revised Manuscript Received August 5, 2003.
Issue or Number:6
DOI:10.1021/bm034120l
Record Number:CaltechAUTHORS:20150109-113118565
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20150109-113118565
Official Citation:Mechanism for the Phase Transition of a Genetically Engineered Elastin Model Peptide (VPGIG)40 in Aqueous Solution Tetsuji Yamaoka, Takumi Tamura, Yuuki Seto, Tomoko Tada, Shigeru Kunugi, and David A. Tirrell Biomacromolecules 2003 4 (6), 1680-1685
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:53477
Collection:CaltechAUTHORS
Deposited By: Katherine Johnson
Deposited On:15 Jan 2015 19:21
Last Modified:10 Nov 2021 20:02

Repository Staff Only: item control page