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• W2025691086 endingPage "181" @default.
• W2025691086 startingPage "169" @default.
• W2025691086 abstract "A thermodynamic approach is proposed to quantitatively analyze the binding isotherms of peptides to model membranes as a function of one adjustable parameter, the actual peptide charge in solution zp+. The main features of this approach are a theoretical expression for the partition coefficient calculated from the molar free energies of the peptide in the aqueous and lipid phases, an equation proposed by S. Stankowski [(1991) Biophysical Journal, Vol. 60, p. 341] to evaluate the activity coefficient of the peptide in the lipid phase, and the Debye-Hückle equation that quantifies the activity coefficient of the peptide in the aqueous phase. To assess the validity of this approach we have studied, by means of steady-state fluorescence spectroscopy, the interaction of basic amphipathic peptides such as melittin and its dansylcadaverine analogue (DNC-melittin), as well as a new fluorescent analogue of substance P, SP (DNC-SP) with neutral phospholipid membranes. A consistent quantitative analysis of each binding curve was achieved. The zp+ values obtained were always found to be lower than the physical charge of the peptide. These zp+ values can be rationalized by considering that the peptide charged groups are strongly associated with counterions in buffer solution at a given ionic strength. The partition coefficients theoretically derived using the zp+ values were in agreement with those deduced from the Gouy-Chapman formalism. Ultimately, from the zp+ values the molar free energies for the free and lipid-bound states of the peptides have been calculated. © 1997 John Wiley & Sons, Inc. Biopoly 42: 169–181, 1997" @default.
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• W2025691086 date "1997-08-01" @default.
• W2025691086 modified "2023-10-17" @default.
• W2025691086 title "Binding of basic amphipathic peptides to neutral phospholipid membranes: A thermodynamic study applied to dansyl-labeled melittin and substance P analogues" @default.
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• W2025691086 doi "https://doi.org/10.1002/(sici)1097-0282(199708)42:2<169::aid-bip6>3.0.co;2-l" @default.
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