Analysis of the Thiol Adduction of Linoleate 9,10-Dihydroxy-11<i>E</i>‑13-ketones of the Mammalian Skin Barrier and Their Cyclization to Hemiketals.

ABSTRACT: Enzymic transformations of esterified linoleate (C18:2ω6) in acylceramides help to seal the mammalian skin permeability barrier by promoting Michael addition to protein thiols via the synthesis of 9,10-trans-epoxy-11E-13-oxo and 9,10-erythro-dihydroxy-11E-13-oxo oxidation products. In modeling the conjugation of these oxidized linoleates with cysteine and glutathione, we observed anomalous chromatographic and proton NMR results for the thiol conjugates of the dihydroxy-ketones. Adduction eliminates the 11,12 double bond and allows spontaneous C9-C13 cyclization to hemiketal derivatives. This produces a polar diastereomer that chromatographs as interconverting hemiketal species and a less polar diastereomer favored as a single hemiketal and stereochemically pure

SUBMITTER: Brash AR 

PROVIDER: S-EPMC12423870 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature