Stereochemistry matters: Inhibition of carbonic anhydrase II by amino acid derived sulfamates depends on their absolute configuration

Aminoalcohols were converted into the corresponding enantiomeric phenylsulfonamide sulfamates. These compounds proved to be inhibitors of carbonic anhydrase II. Interestingly, a sulfamate derived from (S)-tryptophan was no inhibitor at all while its (R) configurated enantiomer was an excellent inhib...

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Bibliographic Details
Published in:European journal of medicinal chemistry reports 2024-08, Vol.11, p.100162, Article 100162
Main Authors: Denner, Toni C., Klett, Elsa L., Heise, Niels V., Csuk, René
Format: Article
Language:English
Subjects:
Carbonic anhydrase II
Inhibitor
Sulfamates
Sulfonamides
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Summary:Aminoalcohols were converted into the corresponding enantiomeric phenylsulfonamide sulfamates. These compounds proved to be inhibitors of carbonic anhydrase II. Interestingly, a sulfamate derived from (S)-tryptophan was no inhibitor at all while its (R) configurated enantiomer was an excellent inhibitor of carbonic anhydrase II (CA II). A rationale can be deduced from molecular modeling studies. The sulfamates derived from (R) or (S) proline held very low inhibition constants for this enzyme as Ki = 0.77 μM and 0.70 μM, respectively. [Display omitted] •Aminoalcohols were converted into the enantiomeric phenylsulfonamide sulfamates.•These compounds proved to be inhibitors of carbonic anhydrase II.•Inhibitory activity depends on both bulkiness and absolute configuration.•The sulfamates from (R) and (S) proline held Ki = 0.77 μM and 0.70 μM, respectively.
ISSN:2772-4174
2772-4174
DOI:10.1016/j.ejmcr.2024.100162