The Conformational Changes of Bovine Serum Albumin at the Air/Water Interface: HDX-MS and Interfacial Rheology Analysis.

ABSTRACT: The characterization and dynamics of protein structures upon adsorption at the air/water interface are important for understanding the mechanism of the foamability of proteins. Hydrogen-deuterium exchange, coupled with mass spectrometry (HDX-MS), is an advantageous technique for providing conformational information for proteins. In this work, an air/water interface, HDX-MS, for the adsorbed proteins at the interface was developed. The model protein bovine serum albumin (BSA) was deuterium-labeled at the air/water interface in situ for different predetermined times (10 min and 4 h), and then the resulting mass shifts were analyzed by MS. The results indicated that peptides 54-63, 227-236, and 355-366 of BSA might be involved in the adsorption to the air/water interface. Moreover, the residu

SUBMITTER: Han F 

PROVIDER: S-EPMC10137346 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature