| Autor: |
Allen S; School of Pharmacy, University of Nottingham, NG7 2RD, UK. stephanie.allen@nottingham.ac.uk, Rigby-Singleton SM, Harris H, Davies MC, O'Shea P |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemical Society transactions [Biochem Soc Trans] 2003 Oct; Vol. 31 (Pt 5), pp. 1052-7. |
| DOI: |
10.1042/bst0311052 |
| Abstrakt: |
In recent years, considerable attention has focused upon the biological applications of the atomic force microscope (AFM), and in particular in its ability to explore biomolecular interaction events at the single molecule level. Such measurements can provide considerable advantages, as they remove the data averaging inherent in other biophysical/biochemical approaches that record measurements over large ensembles of molecules. To this end AFM has been used for both the high-resolution imaging of a range of individual biological molecules and their complexes, and to record interaction forces between single interacting molecules. In a recently initiated project we have begun to utilize these approaches to explore the interactions of a range of biologically important peptides with model and cell membrane surfaces. In this review, the potential value of AFM for the investigation of a range of biomolecular interaction events will be discussed, but highlighting in particular its potential for the study of interactions of peptides/proteins with biological membranes. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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