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Conformational Stability and Activity of Circular Enterocin AS-48 Derivatives
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Título :
Conformational Stability and Activity of Circular Enterocin AS-48 Derivatives |
Autor :
Sánchez-Hidalgo, Marina
Fernández-Escamilla, Ana Mª
Martínez-Bueno, Manuel
Valdivia, Eva
Serrano, Luis
Maqueda, Mercedes |
Editor :
Bentham Science Publishers |
Departamento:
Departamentos de la UMH::Bioquímica y Biología Molecular |
Fecha de publicación:
2010-06 |
URI :
https://hdl.handle.net/11000/39237 |
Resumen :
Four AS-48 mutants (Trp24Ala, Gly13Lys, Leu40Lys and Ala53Ser) were obtained by site-directed mutagenesis.
The minimal inhibitory concentration of each peptide showed that only residue Trp24 was unquestionably involved in
the biological activity. Guanidine hydrochloride-induced unfolding assays showed a three-state transition denaturation
process, suggesting a molten-globule-like conformation after the first transition.
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Palabras clave/Materias:
Circular antimicrobial peptides
Site-directed mutagenesis
Lactic-acid bacteria
Enterococci |
Tipo de documento :
info:eu-repo/semantics/article |
Derechos de acceso:
info:eu-repo/semantics/closedAccess |
DOI :
https://doi.org/10.2174/092986610791190390 |
Publicado en:
Protein & Peptide Letters, Vol. 17, Nº 6 (2010) |
Aparece en las colecciones:
Artículos - Bioquímica y Biología Molecular
|
La licencia se describe como: Atribución-NonComercial-NoDerivada 4.0 Internacional.
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