Induced conformational states of amphipathic peptides in aqueous/lipid environments Article

Blondelle, SE, Ostresh, JM, Houghten, RA et al. (1995). Induced conformational states of amphipathic peptides in aqueous/lipid environments . BIOPHYSICAL JOURNAL, 68(1), 351-359. 10.1016/S0006-3495(95)80194-3

cited authors

  • Blondelle, SE; Ostresh, JM; Houghten, RA; Pérez-Payá, E

authors

abstract

  • Specific conformational effects have been reported for amphipathic model peptides upon binding of defined hydrophobic domains to nonpolar stationary phases during reversed-phase high performance liquid chromatography (RP-HPLC). Such induced conformations are found to be especially pronounced for peptides that are amphipathic in an alpha-helical conformation. Such induced amphipathic conformations resulted in substantially later elution than predicted using amino acid-based retention coefficients. In the present study, the induced conformational behavior of model peptides observed during RP-HPLC was correlated with their secondary structure as determined by circular dichroism (CD) spectroscopy in both aqueous solution and C18-mimetic environments. The experimental retention times of the peptides studied were found to correlate with their CD spectra in the presence of lipids, whereas a poor correlation was observed with their CD spectra in the presence of trifluoroethanol. A new approach was developed to evaluate the induction of secondary structure in peptides due to interactions at aqueous/lipid interfaces, which involves the measurement of the CD ellipticities of peptides bound to a set of C18-coated quartz plates. An excellent correlation was found in this environment between the RP-HPLC retention times and CD ellipticities of the bound peptides. © 1995, The Biophysical Society. All rights reserved.

publication date

  • January 1, 1995

published in

Digital Object Identifier (DOI)

start page

  • 351

end page

  • 359

volume

  • 68

issue

  • 1