期刊
LANGMUIR
卷 24, 期 18, 页码 9923-9928出版社
AMER CHEMICAL SOC
DOI: 10.1021/la801695j
关键词
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资金
- NIH [R25 HL069537-06]
- CUNY
- Grove Foundation
We describe a rationally designed peptide with tunable surface activity, where the dynamics of surface activity are an outcome of helical folding. Our rationally designed model peptide is surface-active only as an cc-helix. We apply circular dichroism to show that the folded population can be controlled with changes in electrolyte concentration, and we apply pendant bubble tensiometry to explore dynamic surfactant activity. This study shows a peptide that responds to environmental stimuli with dynamic folding and surface activity. Extending this concept to selective binding peptides will lead to new tools, where dynamic surface activity is coupled to targeted binding.
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