Detalle de: Crystal structure of thioflavin-T and its binding to amyloid fibrils: Insights at the molecular level
| Title | Crystal structure of thioflavin-T and its binding to amyloid fibrils: Insights at the molecular level |
| Abstract |
Combining X-ray data on thioflavin-T and theoretical calculations on its binding to a peptide model for Abeta(1-42) fibrils gives evidence of main stabilizing interactions, which influence the dihedral angle between the two moieties of thioflavin-T and thereby its fluorescence properties; these results shed new light on possible strategies for the design of dyes to bind amyloid fibrils more specifically. |
| Apa Reference | Rodríguez-Rodríguez, C., Rimola, A., Rodríguez-Santiago, L., Ugliengo, P., Álvarez-Larena, Á., Gutiérrez-de-Terán, H., Sodupe, M., & González-Duarte, P. (2010). Crystal structure of thioflavin-T and its binding to amyloid fibrils: insights at the molecular level. Chemical Communications, 46(7), 1156. 10.1039/b912396b |
| Doi | 10.1039/b912396b |
| Publication Date | 2010 |
| Publication Type | Article |
| Researcher | Hugo Gutiérrez de Terán Castañón |
| Ontology | Structural bioinformatics, Experimental structure determination |
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