Dynamic surface activity by folding and unfolding an amphiphilic alpha-helix.
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 alpha-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.
Jain
Vikas
V
Department of Chemical Engineering, The City College of City University of New York, 140th Street and Convent Avenue, New York, NY 10031, USA.
Jimenez
Angela
A
Maldarelli
Charles
C
Tu
Raymond S
RS
D000388:Air; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D002942:Circular Dichroism; D004247:DNA / Q000737:chemistry; D008024:Ligands; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D013499:Surface Properties; D013501:Surface-Active Agents / Q000737:chemistry; D014867:Water / Q000737:chemistry
D008024:Ligands; D010455:Peptides; D011506:Proteins; D013501:Surface-Active Agents; D014867:Water; D004247:DNA