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PubMed2004

Design, synthesis, and in vitro evaluation of inhibitors of human leukocyte elastase based on a functionalized cyclic sulfamide scaffold.

The design of novel functionalized templates capable of binding to the active site of serine proteases could potentially lead to the development of potent and highly selective non-covalent inhibitors of these enzymes. Using the elastase-turkey ovomucoid inhibitor complex and insights gained from earlier work based on the 1,2,5-thiadiazolidin-3-one 1,1 dioxide scaffold (I), a surrogate cyclosulfamide scaffold (II) was used for the first time in the design of reversible inhibitors of human leukocyte elastase. Compounds 7 and 8 were found to be micromolar reversible inhibitors of the enzyme.

Cyclization↗
PubMed2004

Sulfamide derivatives as transition state analogue inhibitors for carboxypeptidase A.

3-Phenyl-2-sulfamoyloxypropionic acid (2), 2-benzyl-3-sulfamoylpropionic acid (3), and N-(N-hydroxysulfamoyl)phenylalanine (5) have been synthesized and evaluated as inhibitors for carboxypeptidase A (CPA) to find that they inhibit the enzyme competitively with the Ki values in the microM range, suggesting that their binding modes to CPA are analogous to each other, and resemble the binding mode of N-sulfamoylphenylalanine (1) that has been established by the X-ray crystallographic method to form a complex with CPA in a manner reminiscent of the binding of a transition state in the catalytic pathway. It was concluded thus that they are a new type of transition state analogue inhibitors for CPA. (R)-N-Hydroxy-N-sulfamoyl-beta-phenylalanine (8) was shown to be also a potent CPA inhibitor (Ki = 39 microM), the high potency of which may be ascribed to the involvement of the hydroxyl in the binding of CPA, most likely forming bidentate coordinative bonds to the zinc ion in CPA together with the sulfamoyl oxygen atom.

Carboxypeptidases A↗
PubMed2004

[Genotypic resistance to sulfamide drugs among patients with Pneumocystis jiroveci pneumonia].

BACKGROUND AND OBJECTIVE: The absence of culture methods to recognize the presence of resistance to sulfa or sulfone drugs in Pneumocystis jiroveci has led to develop molecular techniques based on the identification of mutations in the dihydropteroate synthase gene (DHPS). The aim of this study was to determine the frequency of these mutations in our geographical area, since in Spain there is no information concerning this issue. PATIENTS AND METHOD: The study included all Pneumocystis pneumonia cases identified in our hospital during two years. Diagnosis was made by nested PCR in bronchoalveolar lavage samples. DHPS-3 and DHPS-4 primers were used to amplify the DHPS gene and mutations associated with sulfa resistance were identified using a restriction fragment length polymorphism assay. RESULTS: In 9 out of the 12 cases identified, DHPS could be amplified (75%) from which 3 (33.3%) showed some mutation linked to sulfa resistance. CONCLUSIONS: In our area, we have found a relatively high frequency of pneumonia caused by P. jiroveci's strains with mutations associated with sulfa resistance.

Adult↗
PubMed1985

Resolution and absolute configuration of the potent dopamine agonist N,N-diethyl-N'-[(3 alpha, 4a alpha, 10a beta)-1,2,3,4,4a,5,10,10a- -octahydro-6-hydroxy-1-propyl-3-benzo[g]quinolinyl]sulfamide.

The synthesis and preliminary pharmacological evaluation of the optical antipodes of the title compound (+/-)-1 (CV 205-502) is presented. The dopaminomimetic activity is shown to reside entirely in the (-) enantiomer. Crystallographic analysis has proven that the absolute configuration of the active (-) enantiomer corresponds to that of its ergoline analogue 3 (CQ 32-084) and of apomorphine (5).

Aminoquinolines↗
PubMed2002

Sulfamide-based inhibitors for carboxypeptidase A. Novel type transition state analogue inhibitors for zinc proteases.

N-Sulfamoylphenylalanine and its derivatives having varied alkyl groups on the terminal amino group were designed rationally as transition state analogue inhibitors for carboxypeptidase A (CPA) and synthesized. In CPA inhibitory assays the parent compound having the (S)-configuration, i.e., (S)-1a, showed potent inhibitory activity with the K(i) value of 0.64 microM. Its enantiomer was shown to be much less potent (K(i) = 470 microM). Introduction of an alkyl group such as methyl or isopropyl group on the terminal amino group of (S)-1a lowered the inhibitory potency drastically. Introduction of a methyl group on the internal amino group of (S)-1a also caused a drastic reduction of the inhibitory activity. The structure of the CPA x(S)-1a complex determined by single-crystal X-ray diffraction reveals that the sulfamoyl moiety interacts with the zinc ion and functional groups at the active site of CPA, which is reminiscent of the postulated stabilization mode of a tetrahedral transition state in the CPA-catalyzed hydrolysis of a peptide substrate. On the basis of the design rationale and the binding mode of (S)-1a to CPA shown by X-ray crystallographic analysis, the present inhibitors are inferred to be a novel type of transition state analogue inhibitor for CPA.

Carboxypeptidases↗