PH-dependent deformations of the energy landscape of avidin-like proteins investigated by single molecule force spectroscopy.

ABSTRACT: Avidin and avidin-like proteins are widely used in numerous techniques since the avidin-biotin interaction is known to be very robust and reliable. Within this study, we investigated this bond at the molecular level under harsh conditions ranging from very low to very high pH values. We compared avidin with streptavidin and a recently developed avidin-based mutant, chimeric avidin. To gain insights of the energy landscape of these interactions we used a single molecule approach and performed the Single Molecule Force Spectroscopy atomic force microscopy technique. There, the ligand (biotin) is covalently coupled to a sharp AFM tip via a distensible hetero-bi-functional crosslinker, whereas the receptor of interest is immobilized on the probe surface. Receptor-ligand complexes are formed an

SUBMITTER: Kohler M 

PROVIDER: S-EPMC6271454 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature