Interaction of cyclic and linear Labaditin peptides with anionic and zwitterionic micelles
| Autor: | Rodrigo G. Stábeli, Luís G. Dias, Eduardo Maffud Cilli, Pietro Ciancaglini, Rosângela Itri, Léo Degrève, Carlos Alessandro Fuzo, Sandra Barbosa |
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| Přispěvatelé: | Universidade Estadual Paulista (Unesp) |
| Rok vydání: | 2014 |
| Předmět: |
Anions
Molecular dynamic Labaditin Peptide Circular dichroism Molecular Dynamics Simulation Micelle Peptides Cyclic Fluorescence Biomaterials chemistry.chemical_compound Molecular dynamics Colloid and Surface Chemistry Tryptophan fluorescence Organic chemistry Sodium dodecyl sulfate Micelles chemistry.chemical_classification Aqueous medium MECANISMO VEGETAL Circular Dichroism Surfaces Coatings and Films Electronic Optical and Magnetic Materials Crystallography chemistry Cyclic peptide lipids (amino acids peptides and proteins) Peptides |
| Zdroj: | Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual) Universidade de São Paulo (USP) instacron:USP Currículo Lattes Repositório Institucional da UNESP Universidade Estadual Paulista (UNESP) instacron:UNESP |
| ISSN: | 1095-7103 |
| Popis: | Made available in DSpace on 2015-05-15T13:30:14Z (GMT). No. of bitstreams: 0 Previous issue date: 2014 Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) 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 λmax 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 β-structure upon interaction with SDS and LPC, albeit with structural differences in each medium. Universidade Estadual Paulista Júlio de Mesquita Filho, Departamento de Bioquímica e Tecnologia Química, Instituto de Química de Araraquara, Araraquara, Rua Professor Francisco Degni, 55, Jardim Quitandinha, CEP 14800060, SP, Brasil Universidade Estadual Paulista Júlio de Mesquita Filho, Departamento de Bioquímica e Tecnologia Química, Instituto de Química de Araraquara, Araraquara, Rua Professor Francisco Degni, 55, Jardim Quitandinha, CEP 14800060, SP, Brasil Departamento de Química, FFCLRP-USP, 14040-901 Ribeirão Preto, SP, Brazil Departamento de Bioquímica e Biotecnologia, IQ-UNESP-Univ. Estadual Paulista, Araraquara, SP, Brazil 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 Departamento de Física Aplicada, Instituto de Física, IF-USP, São Paulo, SP, Brazil |
| Databáze: | OpenAIRE |
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