Binding interactions between human angiotensin II [4474-91-3] and dipalmitoylphosphatidylcholine [2644-64-6] bilayer vesicles were detected by measuring the selective 1H spin-lattice relaxation rates of arom. protons within the peptide. Involvement of the imidazole moiety of the histidine residue in position 6 was demonstrated by the pH dependence of the NMR functions. A lower limit of the binding const. was estd. to be 78.12 mol-1 dm3 for the interaction involving nonionic intermol. forces between arom. residues and the lipid matrix.
SELECTIVE H-1-NMR RELAXATION INVESTIGATIONS OF MEMBRANE-BOUND DRUGS INVITRO .2. ANGIOTENSIN-II / G., Valensin; Delfini, Maurizio; E., Gaggelli. - In: BIOPHYSICAL CHEMISTRY. - ISSN 0301-4622. - STAMPA. - 24:1(1986), pp. 25-31. [10.1016/0301-4622(86)85055-4]
SELECTIVE H-1-NMR RELAXATION INVESTIGATIONS OF MEMBRANE-BOUND DRUGS INVITRO .2. ANGIOTENSIN-II
DELFINI, Maurizio;
1986
Abstract
Binding interactions between human angiotensin II [4474-91-3] and dipalmitoylphosphatidylcholine [2644-64-6] bilayer vesicles were detected by measuring the selective 1H spin-lattice relaxation rates of arom. protons within the peptide. Involvement of the imidazole moiety of the histidine residue in position 6 was demonstrated by the pH dependence of the NMR functions. A lower limit of the binding const. was estd. to be 78.12 mol-1 dm3 for the interaction involving nonionic intermol. forces between arom. residues and the lipid matrix.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
