In silico molecular docking analysis of antibiotic resistant enzymes from extended spectrum β-lactamase (ESBL) producing klebsiella pneumonia

Antibiotic resistance is an increasing global public health problem, creating significant challenges in treating hospital-acquired infections. One of the main reasons for the spread of this resistance is the inactivation of beta-lactam antibiotics by bacteria through the production of beta-lactamase enzymes. Klebsiella pneumoniae is a major pathogen that produces extended-spectrum beta-lactamases (ESBLs), leading to severe infections, particularly in immunocompromised individuals and patients in intensive care units. ESBL enzymes such as SHV, CTX-M, and TEM are commonly involved in the resistance mechanisms of this bacterium and hold significant clinical importance. The aim of this study is to identify potential new lead molecules that can act as inhibitors of SHV, CTX-M, and TEM enzymes, thus contributing to the development of alternative therapeutic strategies against antibiotic resistance. To achieve this, computational methods were employed to screen small molecules with potential biological activity from the ZINC database. In silico approaches, particularly molecular docking and molecular dynamics simulations, were used to evaluate the interactions of candidate molecules with SHV, CTX-M, and TEM enzymes. The findings suggest that some molecules exhibit high binding affinity to these enzymes and may potentially inhibit their activity. Experimental testing and clinical evaluation of these molecules could significantly contribute to the development of new drugs for treating infections caused by ESBL-producing K. pneumoniae.