Tunable Thermoresponsiveness of Resilin via Coassembly with Rigid Biopolymers

Whittaker, J, Dutta, N, Knott, R, McPhee, G, Voelcker, N, Elvin, C, Hill, A and Choudhury, N 2015, 'Tunable Thermoresponsiveness of Resilin via Coassembly with Rigid Biopolymers', Langmuir, vol. 31, no. 32, pp. 8882-8891.


Document type: Journal Article
Collection: Journal Articles

Title Tunable Thermoresponsiveness of Resilin via Coassembly with Rigid Biopolymers
Author(s) Whittaker, J
Dutta, N
Knott, R
McPhee, G
Voelcker, N
Elvin, C
Hill, A
Choudhury, N
Year 2015
Journal name Langmuir
Volume number 31
Issue number 32
Start page 8882
End page 8891
Total pages 10
Publisher American Chemical Society
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.
Subject Biomaterials
Chemical Engineering not elsewhere classified
Interdisciplinary Engineering not elsewhere classified
DOI - identifier 10.1021/acs.langmuir.5b01014
Copyright notice © 2015 American Chemical Society.
ISSN 0743-7463
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