A Unified Model for De Novo Design of Elastin-like Polypeptides with Tunable Inverse Transition Temperatures

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, d...

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Bibliographic Details
Published in:Biomacromolecules 2013-08, Vol.14 (8), p.2866-2872
Main Authors: McDaniel, Jonathan R, Radford, D. Christopher, Chilkoti, Ashutosh
Format: Article
Language:English
Subjects:
Algorithms
Amino Acid Sequence
Applied sciences
Elastin - chemistry
Exact sciences and technology
Models, Molecular
Molecular Weight
Natural polymers
Physicochemistry of polymers
Protein Engineering
Proteins
Solutions
Transition Temperature
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Summary: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.
ISSN:1525-7797
1526-4602
DOI:10.1021/bm4007166