Structural insights of WBmDapE and deciphering of potent anti-filarial inhibitors: a state-of-art computational approach.

Lymphatic filariasis (LF) stands as a debilitating tropical ailment, impacting a considerable global populace. Existing drug therapies for LF exhibit limited effectiveness across all parasite stages, thereby accentuating the imperative for novel anti-filarial medications characterized by enhanced prognostic attributes and minimized adverse reactions. A promising avenue involves targeting the microbial enzyme WBmDapE, pivotal in worm survival and intricately linked to the lysine biosynthetic pathway and peptidoglycan cell wall construction.

Computational screening of potential inhibitors targeting MurF of Brugia malayi Wolbachia through multi-scale molecular docking, molecular dynamics and MM-GBSA analysis.

Lymphatic filariasis is a parasitic disease caused by the worms Wuchereria bancrofti, Brugia malayi and Brugia timori. Three anti-filarial drugs namely Diethylcarbamazine, Ivermectin and Albendazole and their combinations are used as the control strategies for filariasis. The disease has received much attention in drug discovery due to the unavailability of vaccines and the toxic pharmaceutical properties of the existing drugs.

Water Mapping and Scoring Approaches to Predict the Role of Hydration Sites in the Binding Affinity of PAK1 Inhibitors.

Aim: This study aims to develop and establish a computational model that can identify potent molecules for p21-activating kinase 1 (PAK1) Background: PAK1 is a well-established drug target that has been explored for various therapeutic interventions. Control of this protein requires an indispensable inhibitor to curb the structural changes and subsequent activation of signalling effectors responsible for the progression of diseases, such as cancer, inflammatory, viral, and neurological disorders.

Objective: The study aims to establish a computational model that could identify active molecules which will further provide a platform for developing potential PAK1 inhibitors.

Molecular evolution, binding site interpretation and functional divergence of aspartate semialdehyde dehydrogenase.

Aspartate Semialdehyde Dehydrogenase (ASDH) is an important enzyme essential for the viability of pathogenic microorganisms. ASDH is mainly involved in amino acid and cell wall biosynthesis of microorganisms, hence it is considered to be a promising target for drug design. This enzyme depicts similar mechanistic function in all microorganisms; although, the kinetic efficiency of an enzyme differs according to their active site residual composition.

Evolutionary significance and functional characterization of streptomycin adenylyltransferase from .

Complete functional annotations of proteins are essential to understand the role and mechanisms in pathogenesis. Aminoglycoside nucleotidyltransferases are the subclasses of aminoglycosides modifying enzymes conferring resistance to organisms. Insight into the structural and functional understanding of nucleotidyltransferase family protein provides vital information to combat pathogenesis.

Identification of Pak1 inhibitors using water thermodynamic analysis.

p21-activated kinases (Paks) play an integral component in various cellular diverse processes. The full activation of Pak is dependent upon several serine residues present in the N-terminal region, a threonine present at the activation loop, and finally the phosphorylation of these residues ensure the complete activation of Pak1. The present study deals with the identification of novel potent candidates of Pak1 using computational methods as anti-cancer compounds.