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Type: Journal article
Title: Tunable thermoresponsiveness of resilin via coassembly with rigid biopolymers
Author: Whittaker, J.
Dutta, N.
Knott, R.
McPhee, G.
Voelcker, N.
Elvin, C.
Hill, A.
Roy Choudhury, N.
Citation: Langmuir: the ACS journal of surfaces and colloids, 2015; 31(32):8882-8891
Publisher: American Chemical Society
Issue Date: 2015
ISSN: 0743-7463
Statement of
Jasmin L. Whittaker, Naba K. Dutta, Robert Knott, Gordon McPhee, Nicolas H. Voelcker, Chris Elvin, Anita Hill, and Namita Roy Choudhury
Abstract: The ability to tune the thermoresponsiveness of recombinant resilin protein, Rec1-resilin, through a facile coassembly system was investigated in this study. The effects of change in conformation and morphology with time and the responsive behavior of Rec1-resilin in solution were studied in response to the addition of a rigid model polypeptide (poly-l-proline) or a hydrophobic rigid protein (Bombyx mori silk fibroin). It was observed that by inducing more ordered conformations and increasing the hydrophobicity the lower critical solution temperature (LCST) of the system was tuned to lower values. Time and temperature were found to be critical parameters in controlling the coassembly behavior of Rec1-resilin in both the model polypeptide and more complex protein systems. Such unique properties are useful for a wide range of applications, including drug delivery and soft tissue engineering applications.
Keywords: Hydrophobic and Hydrophilic Interactions
Description: Published: July 15, 2015
Rights: © 2015 American Chemical Society
DOI: 10.1021/acs.langmuir.5b01014
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Chemical Engineering publications

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