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Self-Assembly of Hydrogels From Elastin-Mimetic Block Copolymers

Published online by Cambridge University Press:  01 February 2011

Elizabeth R. Wright
Affiliation:
Department of Chemistry, Emory University, Atlanta, GA 30322
R. Andrew McMillan
Affiliation:
Department of Chemistry, Emory University, Atlanta, GA 30322
Alan Cooper
Affiliation:
Chemistry Department, University of Glasgow, Glasgow, Scotland, UK
Robert P. Apkarian
Affiliation:
Integrated Microscopy & Microanalytical Facility, Department of Chemistry, Emory University, Atlanta, GA 30322
Vincent P. Conticello
Affiliation:
Department of Chemistry, Emory University, Atlanta, GA 30322
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Abstract

Triblock copolymers have traditionally been synthesized with conventional organic components. However, triblock copolymers could be synthesized by the incorporation of two incompatible protein-based polymers. The polypeptides would differ in their hydrophobicity and confer unique physiochemical properties to the resultant materials. One protein-based polymer, based on a sequence of native elastin, that has been utilized in the synthesis of biomaterials is poly (Valine-Proline-Glycine-ValineGlycine) or poly(VPGVG) [1]. This polypeptide has been shown to have an inverse temperature transition that can be adjusted by non-conservative amino acid substitutions in the fourth position [2]. By combining polypeptide blocks with different inverse temperature transition values due to hydrophobicity differences, we expect to produce amphiphilic polypeptides capable of self-assembly into hydrogels. Our research examines the design, synthesis and characterization of elastin-mimetic block copolymers as functional biomaterials. The methods that are used for the characterization include variable temperature 1D and 2D High-Resolution-NMR, cryo-High Resolutions Scanning Electron Microscopy and Differential Scanning Calorimetry.

Type
Research Article
Copyright
Copyright © Materials Research Society 2002

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