Effect of Ligands on HP-Induced Unfolding and Oligomerization of β-Lactoglobulin.

ABSTRACT: To probe intermediate states during unfolding and oligomerization of proteins remains a major challenge. High pressure (HP) is a powerful tool for studying these problems, revealing subtle structural changes in proteins not accessible by other means of denaturation. Bovine β-lactoglobulin (BLG), the main whey protein, has a strong propensity to bind various bioactive molecules such as retinol and resveratrol, two ligands with different affinity and binding sites. By combining in situ HP-small-angle neutron scattering (SANS) and HP-ultraviolet/visible absorption spectroscopy, we report the specific effects of these ligands on three-dimensional conformational and local changes in BLG induced by HP. Depending on BLG concentration, two different unfolding mechanisms are observed in situ under

SUBMITTER: Minic S 

PROVIDER: S-EPMC7732772 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature