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Online Journal of Veterinary Research 

(Including Medical and Laboratory Research)

Established 1994

ISSN 1328-925X


Volume  28 (3): 123-134, 2024.


Affinity of β-lactams binding on Staphylococcus aureus


Tanzeer Kaura (Ph.D), Sonal Jamwalb(M.Sc), Neeraj Khullarb(Ph.D), S. S. Baric(Ph.D)


aDepartments of Biophysics, bBiotechnology and cChemistry, Panjab University, Chandigarh




Kaura T, Jamwalb S, Khullarb N, Baric SS., Affinity of β-lactams binding on Staphylococcus aureus, Onl J Vet Res., 28 (3): 123-134, 2024. β-lactamases and mutations in penicillin binding proteins may induce β-lactam resistant microorganisms. Structural similarity of β-lactam antibiotics with D-alanyl-D-alanine enhances active site of penicillin binding proteins. Affinity of 8 new β-lactams with penicillin binding and Ser/Thr kinase associated domain (PASTA) protein by docking simulation is described. All compounds showed negative free energies of binding suggestive of strong interaction with PBP 2b. β-lactams had strong interaction with PASTA protein, greater than with penicillin. In Vitro antibacterial tests showed that compound BL1, BL2, BL6 and BL7 presented strong interactions with PASTA with an inhibition comparable to penicillin.


KEY WORDS- β-lactams, Penicillin binding proteins (PBPs), Penicillin binding protein and Ser/Thr kinase associated domain (PASTA domain),Serine/Threonine Kinases (Ser/Thr kinases), staphylococcus aureus, Penicillin, Docking Simulations