Conductance Changes in Bovine Serum Albumin Caused by Drug-Binding Triggered Structural Transitions.

ABSTRACT: Proteins, due to their binding selectivity, are promising candidates for fabricating nanoscale bio-sensors. However, the influence of structural change on protein conductance caused by specific protein-ligand interactions and disease-induced degeneration still remains unknown. Here, we excavated the relationship between circular dichroism (CD) spectroscopy and conductive atomic force microscopy (CAFM) to reveal the effect of the protein secondary structures changes on conductance. The secondary structure of bovine serum albumin (BSA) was altered by the binding of drugs, like amoxicillin (Amox), cephalexin (Cefa), and azithromycin (Azit). The CD spectroscopy shows that the α-helical and β-sheet content of BSA, which varied according to the molar ratio between the drug and BSA, changed by up

SUBMITTER: Yu J 

PROVIDER: S-EPMC6479529 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature