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OJVRTM
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
ABSTRACT
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