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Effects of salt and denaturant on structure of the amino terminal alpha-helical segment of an antibacterial peptide dermaseptin and its binding to model membranes.
Indian J Biochem Biophys ; 2001 Jun; 38(3): 142-8
Artículo en Inglés | IMSEAR | ID: sea-28273
ABSTRACT
The amino terminal 1-18 domain of dermaseptin s is an important determinant of its structure as well as the antibacterial activity. A thorough investigation on the structure of the 18-residue peptide (D18) and its binding to model membranes in presence of salt and denaturant guanidinium chloride has been carried out. In presence of salt, there is an increase in the fraction of peptide molecules in helical conformation. In presence of the denaturant, D18 is unordered, but addition of the structure-promoting solvent trifluoroethanol results in a transition to the helical conformation. In presence of denaturant, the peptide is unordered, but binding to lipid vesicles is not abolished. Investigation of model membrane permeabilizing ability of the peptide in solutions containing various proportions of sodium chloride and guanidinium chloride indicates that vesicle permeabilization parallels extent of binding. The peptide thus binds to lipid vesicles in an unfolded state. Since the peptide has propensity to fold into a helical conformation, lipid induced transition to a helical structure occurs, followed by membrane permeabilization as a result of pore formation.
Asunto(s)
Texto completo: Disponible Índice: IMSEAR (Asia Sudoriental) Asunto principal: Biosíntesis de Péptidos / Unión Proteica / Conformación Proteica / Desnaturalización Proteica / Sales (Química) / Espectrofotometría / Factores de Tiempo / Trifluoroetanol / Datos de Secuencia Molecular / Secuencia de Aminoácidos Tipo de estudio: Estudio pronóstico Idioma: Inglés Revista: Indian J Biochem Biophys Año: 2001 Tipo del documento: Artículo

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Texto completo: Disponible Índice: IMSEAR (Asia Sudoriental) Asunto principal: Biosíntesis de Péptidos / Unión Proteica / Conformación Proteica / Desnaturalización Proteica / Sales (Química) / Espectrofotometría / Factores de Tiempo / Trifluoroetanol / Datos de Secuencia Molecular / Secuencia de Aminoácidos Tipo de estudio: Estudio pronóstico Idioma: Inglés Revista: Indian J Biochem Biophys Año: 2001 Tipo del documento: Artículo