The C2 entity of chitosugars is crucial in molecular selectivity of the Vibrio campbellii chitoporin.

ABSTRACT: The marine bacterium Vibrio campbellii expresses a chitooligosaccharide-specific outer-membrane channel (chitoporin) for the efficient uptake of nutritional chitosugars that are externally produced through enzymic degradation of environmental host shell chitin. However, the principles behind the distinct substrate selectivity of chitoporins are unclear. Here, we employed black lipid membrane (BLM) electrophysiology, which handles the measurement of the flow of ionic current through porins in phospholipid bilayers for the assessment of porin conductivities, to investigate the pH dependency of chitosugar-chitoporin interactions for the bacterium's natural substrate chitohexaose and its deacetylated form, chitosan hexaose. We show that efficient passage of the N-acetylated chitohexaose throug

SUBMITTER: Suginta W 

PROVIDER: S-EPMC8608610 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature