Interplay between the hydrophobic effect and dipole interactions in peptide aggregation at interfaces
Author:
Affiliation:
1. Fischell Department of Bioengineering
2. University of Maryland
3. College Park
4. USA
5. Fischell Department of Bioengineering and Biophysics Program
Abstract
Amphipathic octapeptide aggregation at hydrophobic–hydrophilic interfaces is largely driven by backbone dipole interactions in peptide aggregation at interfaces.
Funder
Division of Chemistry
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2016/CP/C5CP05867H
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