dorzolamide and Dermatomycoses

dorzolamide has been researched along with Dermatomycoses* in 1 studies

Other Studies

1 other study(ies) available for dorzolamide and Dermatomycoses

Article	Year
Molecular cloning, characterization, and inhibition studies of a β-carbonic anhydrase from Malassezia globosa, a potential antidandruff target. Journal of medicinal chemistry, 2012, Apr-12, Volume: 55, Issue:7 A β-carbonic anhydrase (CA, EC 4.2.1.1) from the fungal pathogen Malassezia globosa has been cloned, characterized, and studied for its inhibition with sulfonamides. This enzyme, designated MG-CA, has significant catalytic activity in the CO(2) hydration reaction and was inhibited by sulfonamides, sulfamates, and sulfamides with K(I) in the nanomolar to micromolar range. Several sulfonamides have also been investigated for the inhibition of growth of M. globosa, M. dermatis, M. pachydermatic, and M. furfur in cultures, whereas a mouse model of dandruff showed that treatment with sulfonamides led to fragmented fungal hyphae, as for the treatment with ketoconazole, a clinically used antifungal agent. These data prompt us to propose MG-CA as a new antidandruff drug target. Topics: Amino Acid Sequence; Animals; Antifungal Agents; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cloning, Molecular; Dermatomycoses; Fungal Proteins; Humans; Isoenzymes; Malassezia; Mice; Microbial Sensitivity Tests; Models, Molecular; Molecular Sequence Data; Recombinant Fusion Proteins; Scalp Dermatoses; Structure-Activity Relationship; Sulfonamides; Sulfonic Acids	2012

Article

Year

Molecular cloning, characterization, and inhibition studies of a β-carbonic anhydrase from Malassezia globosa, a potential antidandruff target.

Journal of medicinal chemistry, 2012, Apr-12, Volume: 55, Issue:7

A β-carbonic anhydrase (CA, EC 4.2.1.1) from the fungal pathogen Malassezia globosa has been cloned, characterized, and studied for its inhibition with sulfonamides. This enzyme, designated MG-CA, has significant catalytic activity in the CO(2) hydration reaction and was inhibited by sulfonamides, sulfamates, and sulfamides with K(I) in the nanomolar to micromolar range. Several sulfonamides have also been investigated for the inhibition of growth of M. globosa, M. dermatis, M. pachydermatic, and M. furfur in cultures, whereas a mouse model of dandruff showed that treatment with sulfonamides led to fragmented fungal hyphae, as for the treatment with ketoconazole, a clinically used antifungal agent. These data prompt us to propose MG-CA as a new antidandruff drug target.

Topics: Amino Acid Sequence; Animals; Antifungal Agents; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cloning, Molecular; Dermatomycoses; Fungal Proteins; Humans; Isoenzymes; Malassezia; Mice; Microbial Sensitivity Tests; Models, Molecular; Molecular Sequence Data; Recombinant Fusion Proteins; Scalp Dermatoses; Structure-Activity Relationship; Sulfonamides; Sulfonic Acids

2012