Abstract
Vancomycin possesses the unusual property of promoting the aggregation of proteins. It also binds to itself (dimerization). Both properties may be related to its antimicrobial activity and we report here procedures to measure them. The position of the negative ellipticity band in the near ultraviolet circular dichroism spectrum of the vancomycin monomer shifts as a function of antibiotic concentration and can be used to readily determine the monomer-dimer equilibrium constant. These measurements complement those performed by high-resolution gel filtration to measure the same process. Aggregation of purified proteins was determined by turbidity measurements. Both dimerization and protein aggregation are influenced by anions whose effectiveness is related to their carboxyl pKa values, thus linking these two properties.
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