Utilize este identificador para referenciar este registo:
https://hdl.handle.net/10316/5850
Título: | Ciprofloxacin interactions with bacterial protein OmpF: Modelling of FRET from a multi-tryptophan protein trimer | Autor: | Fernandes, Fábio Neves, Patrícia Gameiro, Paula Loura, Luís M. S. Prieto, Manuel |
Palavras-chave: | Fluorescence; Fluoroquinolones; Membrane protein; Membrane model system | Data: | 2007 | Citação: | Biochimica et Biophysica Acta (BBA) - Biomembranes. 1768:11 (2007) 2822-2830 | Resumo: | The outer membrane protein F (OmpF) is known to play an important role in the uptake of fluoroquinolone antibiotics by bacteria. In this study, the degree of binding of the fluoroquinolone antibiotic ciprofloxacin to OmpF in a lipid membrane environment is quantified using a methodology based on Förster resonance energy transfer (FRET). Analysis of the fluorescence quenching of OmpF is complex as each OmpF monomer presents two tryptophans at different positions, thus sensing two different distributions of acceptors in the bilayer plane. Specific FRET formalisms were derived accounting for the different energy transfer contributions to quenching of each type of tryptophan of OmpF, allowing the recovery of upper and lower boundaries for the ciprofloxacin-OmpF binding constant (KB). log (KB) was found to lie in the range 3.15-3.62 or 3.58-4.00 depending on the location for the ciprofloxacin binding site assumed in the FRET modelling, closer to the centre or to the periphery of the OmpF trimer, respectively. This methodology is suitable for the analysis of FRET data obtained with similar protein systems and can be readily adapted to different geometries. | URI: | https://hdl.handle.net/10316/5850 | DOI: | 10.1016/j.bbamem.2007.07.016 | Direitos: | openAccess |
Aparece nas coleções: | FFUC- Artigos em Revistas Internacionais |
Ficheiros deste registo:
Ficheiro | Descrição | Tamanho | Formato | |
---|---|---|---|---|
file0991a4be888f45ff971ddd19b95ee83f.pdf | 592.05 kB | Adobe PDF | Ver/Abrir |
Citações SCOPUSTM
33
Visto em 18/mar/2024
Citações WEB OF SCIENCETM
50
32
Visto em 2/mar/2024
Visualizações de página 20
657
Visto em 26/mar/2024
Downloads
254
Visto em 26/mar/2024
Google ScholarTM
Verificar
Altmetric
Altmetric
Todos os registos no repositório estão protegidos por leis de copyright, com todos os direitos reservados.