A unified model for de novo design of elastin-like polypeptides with tunable inverse transition temperatures.

Journal Article, Research Support, N.I.H., Extramural, Research Support, U.S. Gov't, Non-P.H.S.

Elastin-like polypeptides (ELPs) are stimulus-responsive peptide polymers that exhibit inverse temperature phase transition behavior, causing an ELP to aggregate above its inverse transition temperature (T(t)). Although this property has been exploited in a variety of biotechnological applications, de novo design of ELPs that display a specific T(t) is not trivial because the T(t) of an ELP is a complex function of several variables, including its sequence, chain length, polypeptide concentration, and the type and concentration of cosolutes in solution. This paper provides a quantitative model that predicts the T(t) of a family of ELPs (Val-Pro-Gly-Xaa-Gly, where Xaa = Ala and/or Val) from their composition, chain length, and concentration in phosphate buffered saline. This model will enable de novo prediction of the amino acid sequence and chain length of ELPs that will display a predetermined T(t) in physiological buffer within a specified concentration regime, thereby greatly facilitating the design of new ELPs for applications in medicine and biotechnology.

Full Text

Duke Authors

Cited Authors

  • McDaniel, JR; Radford, DC; Chilkoti, A

Published Date

  • August 12, 2013

Published In

Volume / Issue

  • 14 / 8

Start / End Page

  • 2866 - 2872

PubMed ID

  • 23808597

Electronic International Standard Serial Number (EISSN)

  • 1526-4602

Digital Object Identifier (DOI)

  • 10.1021/bm4007166

Language

  • eng

Citation Source

  • PubMed