Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1404390 | Journal of Molecular Structure | 2007 | 13 Pages |
Abstract
The association of basic amphipathic peptides to neutral phospholipid membranes is investigated in terms of binding and partition models. The binding of native and modified melittin to egg-yolk phosphatidylcholine vesicles is studied by steady-state fluorescence spectroscopy. The effect of the ionic strength shows an enhancement of the association as the ionic strength increases. After correction for electrostatic effects by the Gouy-Chapman theory, the melittin binding isotherms could be described by a partition model. In terms of conventional binding mechanisms, which do not take into account electrostatic effects, this would correspond to a negative cooperativity. A plausible way in which the interaction occurs is proposed, based on the calculated Hill coefficient.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Francisco Torrens, Gloria Castellano, AgustÃn Campos, Concepción Abad,