Cholinesterases Activities in Diabetic and Hyperlipidemic Patient

Mahmood, Ahmed; Khalaf, Musab M.; Zainal, Adnan A.

doi:10.5958/0976-5506.2019.03297.2

Cited by 1 publication

(3 citation statements)

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“…This backing route includes the creation of a covalent acyl-intermediate among the catalytic serine and the β-lactam moiety in the enzyme's bocket [7]. Alternatively, the metallo-β-lactamases of class B utilize single or double of the zinc ions for accomplishing the β-lactam braking [7,8].…”

Section: Introductionmentioning

confidence: 99%

“…The β-lactamases Temoniera-1 (TEM-1) 1pzp belongs to the serine β-lactamases of the category A which braking the β-lactam group by developing an acyl-intermediate structure with the catalytic serine in the enzyme pocket [7,8].…”

Section: Introductionmentioning

confidence: 99%

“…Talented approaches include the initiation of non-β-lactam inhibitors; they will be effective versus a broad range of β-lactamases. Various inhibitors have now been defined [11]. Boronic acid derivatives are effective for βlactamases categories A, C and D [12].…”

Section: Introductionmentioning

confidence: 99%

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DOCKING, SYNTHESIS AND Β-Lactamase INHIBITORY ACTIVITY EVALUATION FOR NEW AMIDE COMPOUNDS

Mahmood,

Bahnam

2024

Chemical Problems

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The beta-lactams are recognized as effective antibiotics for treating infections, yet bacterial production of β-lactamase, which hydrolyzes the beta-lactam ring, can render these drugs inactive. Combining these antibiotics with a β-lactamase inhibitor, such as clavulanic acid, mitigates this resistance. In a docking study involving Temoniera-1 (TEM-1), 1pzp, we induced the synthesis of eight amide compounds by reacting acid chloride derivatives with sulphathiazol or oxadiazol amine, forming an amide bond. The newly synthesized compounds were differentiated using physical and spectroscopic methods and verified biologically by estimating their minimum inhibitory concentration (MIC) against four strains of βlactamase G(+)ve and G(-)ve bacteria. Their anti β-lactamase behaviors were then compared with that of clavulanic acid as a co-inhibitor with amoxicillin against the same four strains of bacteria. The results indicate that four of the new amides exhibit excellent anti-β-lactamase activity and contain one or more hydrophobic residues in their structures. Halogen atoms enhance the selectivity of tower β-lactamases. Derivatives of both oxadiazole and sulfathiazole scaffolds show promising anti-β-lactamase activity as nonβ-lactam inhibitors.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%