Conformation of a synthetic antigenic peptide from HIV-1 p24 protein induced by ionic micelles |
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| Authors: | Campana Patricia T Beltramini Leila M Costa-Filho Antonio J Tonarelli Georgina Lottersberger Javier Bianconi M Lucia |
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| Institution: | 1. Departamento de Física e Informática, Instituto de Física de São Carlos, C.P. 369, CEP 13566-970, São Carlos, Brazil;2. Departamento de Química Orgánica, Facultad de Bioquímica y Cs. Biológicas, UNL, Ciudad Universitaria, C.C. 242, CP 3000, Santa Fe, Argentina;3. Departamento de Bioquímica Médica, Instituto de Ciências Biológicas, UFRJ, Prédio do CCS, Bloco E, sala 38, Rio de Janeiro, RJ, CEP 21491-590, Brazil;1. Department of Molecular and Cellular Biochemistry, University of Kentucky College of Medicine, Lexington, KY 40536, USA;2. Department of Neuroscience, University of Kentucky College of Medicine, Lexington, KY 40536, USA;3. University of Kentucky Epilepsy & Brain Metabolism Alliance, University of Kentucky College of Medicine, Lexington, KY 40536, USA;4. Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA;5. Lafora Epilepsy Cure Initiative, University of Kentucky College of Medicine, Lexington, KY 40536, USA;6. Markey Cancer Center, Lexington, KY 40536, USA;1. The Noguchi Institute, 1-9-7, Kaga, Itabashi-Ku, Tokyo 173-0003, Japan;2. Department of Systems Biology in Thromboregulation, Kagoshima University, Graduate School of Medical and Dental Sciences, 8-35-1, Sakuragaoka, Kagoshima-City, Kagoshima 890-8520, Japan |
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| Abstract: | We studied the interaction of the peptide AAMQMLKETINEEAAEWDRVHPVHAGPIA from the HIV-1 p24 protein in the presence of SDS (anionic) and CTABr (cationic) micelles at pH 7.0 by circular dichroism, fluorescence, and electron spin resonance (ESR). The micelles induced secondary structure as well as a blue shift in the tryptophan fluorescence emission, indicating an interaction between the peptide and the micelles. However, different contents of secondary structure elements were found when the peptide interacts with SDS or CTABr micelles. Steady-state anisotropy indicates a constraint on the rotational mobility of the tryptophan residue of the peptide upon interaction with micelles. ESR studies pointed to different locations for the peptide in either micelle. Our results suggested that at least part of the peptide might be located at the hydrophobic core of the CTABr micelles, probably at the C-terminal region, while it is more inserted into the SDS micelles. |
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