Effect of macrocyclic compounds to protein aggregation

Abstract

When studying the affinity of albumin to low molecular weight compounds, an extremely interesting phenomenon was discovered. Some porphyrins and macrocyclic compounds intercalate into the serum albumin blood globule, which leads to an increase in the proportion of β-folding and subsequent protein aggregation. Is it possible that organic molecules, getting into the protein globule, cause a local conformational alpha–beta transition and change the zeta potential of the globule, which later leads to aggregation? We tried to answer this and other questions in this review, based on our own and literary information.