Quantitative measurements of vancomycin binding to self-assembled peptide monolayers on chips by quartz crystal microbalance.
Anal Biochem
; 371(1): 1-9, 2007 Dec 01.
Article
en En
| MEDLINE
| ID: mdl-17919449
ABSTRACT
This paper describes direct binding of a small vancomycin to peptide ligands immobilized on a sensor chip using quartz crystal microbalance. In this study, the binding ligands were composed of three components a molecular recognition element (peptide), a conformationally flexible and hydrophilic linker, and a long-chain alkanethiol. These peptide ligands were used to establish the well-packed, self-assembled monolayers on quartz chips and could be readily synthesized using conventional organic chemistry protocols. Results of quartz crystal microbalance measurements showed that vancomycin specifically associated with the d-Ala-d-Ala-containing peptide with an affinity of 3.2+/-0.3 microM and was, as expected, completely inactive to the self-assembled monolayer presenting l-Ala-l-Ala peptide. The dissociation constant obtained correlated well with values reported in literature and was further confirmed by surface plasmon resonance measurement (2.7+/-0.7 microM). The technique used in this study should be applicable to both peptidyl and nonpeptidyl ligands of greater complexity than that used here. This method is practical, it provides quantitative binding information, and complicated analysis is avoided.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Péptidos
/
Cuarzo
/
Vancomicina
/
Técnicas Biosensibles
/
Antibacterianos
Tipo de estudio:
Diagnostic_studies
/
Guideline
Idioma:
En
Revista:
Anal Biochem
Año:
2007
Tipo del documento:
Article
País de afiliación:
China