Interaction of Phenylalanine with DPPC Model Membranes: More Than a Hydrophobic Interaction

• Published in: The journal of physical chemistry. B Vol. 119; no. 52; pp. 15844 - 15847
• Main Authors: Rosa, A. S, Cutro, A. C, Frías, M. A, Disalvo, E. A
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 31.12.2015
• Subjects: 1,2-Dipalmitoylphosphatidylcholine - analogs & derivatives; 1,2-Dipalmitoylphosphatidylcholine - chemistry; Entropy; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Models, Molecular; Phenylalanine - chemistry; Water - chemistry
• ISSN: 1520-6106; 1520-5207
• DOI: 10.1021/acs.jpcb.5b08490

The negative free energy previously reported is explained by the stabilization of a PC-Phe (phosphocholine-phenylalanine) complex in the presence of water shown by the decrease in the symmetric stretching frequency of the phosphate group of the lipid (PO2 –). An entropic contribution due to the disruption of the water network around the phenyl and in the membrane defect may be invoked. The dipole potential decrease is explained by the orientation of the carboxylate opposing to the CO of the lipids with oxygen moiety toward the low hydrated hydrocarbon core. The symmetric bending frequency of NH3 + group of Phe, decreases in 5.2 cm–1 in relation to water congruent with zeta potential shift to positive values. The Phe to DPPC dissociation constant is K d = 2.23 ± 0.09 mM, from which the free energy change is about −4.54 kcal/mol at 25 °C. This may be due to hydrophobic contributions and two hydrogen bonds.