Fast-scan cyclic voltammetry with thiol-modified mercury electrodes distinguishes native from denatured BSA

Abstract

We studied native and denatured bovine serum albumin (BSA) at bare and dithiothreithol (DTT)-modified hanging mercury drop electrode (HMDE) by fast-scan cyclic voltammetry (fsCV) and chronopotentiometric stripping (CPS) to compare these methods for their ability to recognize changes in BSA structure. Using fsCV and bare HMDE, denatured BSA could be distinguished from its native form only between 10 and 20V/s but at lower resolution than with CPS. At DTT-HMDE denatured BSA was recognized from native BSA in a wider range of scan rates suggesting new possibilities in development of voltammetric protein structure-sensitive sensing.