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Biomacromolecules. 2013 Aug 12;14(8):2866-72. doi: 10.1021/bm4007166. Epub 2013 Jul 11.

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

Author information

1
Department of Biomedical Engineering, Duke University, Durham, North Carolina 27708, United States.

Abstract

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.

PMID:
23808597
PMCID:
PMC3779073
DOI:
10.1021/bm4007166
[Indexed for MEDLINE]
Free PMC Article

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