Evaluation of peptidepeptide interactions using reversed-phase high-performance liquid chromatography Article

Blondelle, SE, Büttner, K, Houghten, RA. (1992). Evaluation of peptidepeptide interactions using reversed-phase high-performance liquid chromatography . JOURNAL OF CHROMATOGRAPHY A, 625(2), 199-206. 10.1016/0021-9673(92)85203-6

cited authors

  • Blondelle, SE; Büttner, K; Houghten, RA

abstract

  • The separation of peptides during RP-HPLC depends mainly upon differential hydrophobic interactions of the individual peptides being separated with the C18 group of the stationary phase. We have examined the behavior of dimeric disulfide-linked model peptides during RP-HPLC in order to study self-induced conformational effects. A set of 18 analogues of the amphipathic α-helical sequence Ac-LKLLKKLLKKLKKLLKKL-NH2 was used for this study. These analogues differed only by the successive replacement of each position with a cysteine. Strong peptidepeptide interactions, occurring through interchain hydrophobic forces, resulted in a presenting face to the C18 group, consisting primarily of lysine residues and, in turn, in early retention times. Three homo-dimers were also found to be strongly α-helical in water as determined by circular dichroism spectroscopy. © 1992.

publication date

  • November 20, 1992

published in

Digital Object Identifier (DOI)

start page

  • 199

end page

  • 206

volume

  • 625

issue

  • 2