Self-Assembled Complexes of Synthetic Polypeptides and Oppositely Charged Low Molecular Weight Surfactants. Solid-State Properties
Abstract
Solid-state properties of the stoichiometric complexes formed by sodium poly(α,L-glutamate) and oppositely charged low molecular weight surfactants (alkyltrimethylammonium bromides) were examined by circular dichroism, infrared, and X-ray diffraction techniques. The polypeptide chains in the complexes were shown to be predominantly in the α-helical conformation at room temperature. At higher temperatures, weakening or disruption of intramolecular hydrogen bonds stabilizing the α-helical conformation was observed. The polypeptide−surfactant complexes were shown to adopt lamellar structures in the temperature range 20−150 °C. The lamellae consist of alternating layers of polyglutamate chains and bimolecular layers of surfactant, with the surfactant alkyl chains aligned perpendicular to the lamellar surfaces and interdigitated.
Additional Information
Copyright © 1996 American Chemical Society. Received July 26, 1995. Publication Date (Web): June 3, 1996. Abstract published in Advance ACS Abstracts, May 1, 1996. We thank Prof. A. B. Zezin (Department of Polymer Science, Chemistry Faculty, Moscow State University, Russia) for fruitful discussions. This work was supported by a grant from the National Science Foundation (DMR 9311658) and by the NSF Materials Research Science and Engineering Center at the University of Massachusetts.Additional details
- Eprint ID
- 53448
- Resolver ID
- CaltechAUTHORS:PONm1996
- DMR 9311658
- NSF
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