Dynamic surface activity by folding and unfolding an amphiphilic alpha-helix.

Dynamic surface activity by folding and unfolding an amphiphilic alpha-helix.
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DOI:
10.1021/la801695j
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发表时间:
2008-09-16
期刊:
Langmuir : the ACS journal of surfaces and colloids
影响因子:
--
通讯作者:
Tu RS
Tu RS
中科院分区:
其他
文献类型:
--
作者:
Jain V;Jimenez A;Maldarelli C;Tu RS

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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 α-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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