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Interaction of cyclic and linear Labaditin peptides with anionic and zwitterionic micelles.
Barbosa, S C; Cilli, E M; Dias, L G; Fuzo, C A; Degrève, L; Stabeli, R G; Itri, R; Ciancaglini, P.
Afiliación
  • Barbosa SC; Departamento de Química, FFCLRP-USP, 14040-901 Ribeirão Preto, SP, Brazil.
  • Cilli EM; Departamento de Bioquímica e Biotecnologia, IQ-UNESP-Univ. Estadual Paulista, Araraquara, SP, Brazil.
  • Dias LG; Departamento de Química, FFCLRP-USP, 14040-901 Ribeirão Preto, SP, Brazil.
  • Fuzo CA; Departamento de Química, FFCLRP-USP, 14040-901 Ribeirão Preto, SP, Brazil.
  • Degrève L; Departamento de Química, FFCLRP-USP, 14040-901 Ribeirão Preto, SP, Brazil.
  • Stabeli RG; Centro de Estudos de Biomoléculas Aplicadas a Medicina (CEBio), Núcleo de Saúde (NUSAU), Universidade Federal de Rondônia (UNIR), Fundação Oswaldo Cruz - Fundação Oswaldo Cruz - Rondônia (FIOCRUZ), 76812-245 Porto Velho, RO, Brazil.
  • Itri R; Departamento de Física Aplicada, Instituto de Física, IF-USP, São Paulo, SP, Brazil.
  • Ciancaglini P; Departamento de Química, FFCLRP-USP, 14040-901 Ribeirão Preto, SP, Brazil. Electronic address: pietro@ffclrp.usp.br.
J Colloid Interface Sci ; 438: 39-46, 2015 Jan 15.
Article en En | MEDLINE | ID: mdl-25454423
Conformational changes of the cyclic (Lo) peptide Labaditin (VWTVWGTIAG) and its linear analogue (L1) promoted by presence of anionic sodium dodecyl sulfate (SDS) and zwitterionic L-α-Lysophosphatidylcholine (LPC) micelles were investigated. Results from λ(max) blue-shift of tryptophan fluorescence emission combined with Stern-Volmer constants values and molecular dynamics (MD) simulations indicated that L1 interacts with SDS micelles to a higher extent than does Lo. Further, the MD simulation demonstrated that both Lo and L1 interact similarly with LPC micelles, being preferentially located at the micelle/water interface. The peptide-micelle interaction elicits conformational changes in the peptides. Lo undergoes limited modifications and presents unordered structure in both LPC and SDS micelles. On the other hand, L1 displays a random-coil structure in aqueous medium, pH 7.0, and it acquires a ß-structure upon interaction with SDS and LPC, albeit with structural differences in each medium.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos / Péptidos Cíclicos / Micelas Idioma: En Revista: J Colloid Interface Sci Año: 2015 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Estados Unidos
Texto completo
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Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos / Péptidos Cíclicos / Micelas Idioma: En Revista: J Colloid Interface Sci Año: 2015 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Estados Unidos