Air-Water Interfacial Adsorption of the Chaperone Protein DNAJB6b.

ABSTRACT: Aberrant protein aggregation into amyloid fibrils is often catalyzed by interfaces. Therefore, it is important to characterize the surface activity of chaperone proteins having the ability to suppress amyloid formation. The air-water interface is of large practical significance in experimental setups used to study aggregation kinetics in vitro, but in addition, the binding of chaperones to hydrophobic patches on their clients may also be considered as a consequence of interfacial interactions. Here, we have studied the air-water interfacial adsorption of the human chaperone protein DNAJB6b by using hanging drop tensiometry. The dynamic surface tension exhibited a characteristic pattern in a concentration-dependent manner. First, there was an induction period during which the surface

SUBMITTER: Pallbo J 

PROVIDER: S-EPMC12312157 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature