Toxoplasma gondii is an intracellular Apicomplexan parasite and a causative agent of toxoplasmosis in human. It causes encephalitis, uveitis, chorioretinitis, and congenital infection. T. gondii invades the host cell by forming a moving junction (MJ) complex. This complex formation is initiated by intermolecular interactions between the two secretory parasitic proteins-namely, apical membrane antigen 1 (AMA1) and rhoptry neck protein 2 (RON2) and is critically essential for the host invasion process. By this study, we propose two potential leads, NSC95522 and NSC179676 that can efficiently target the AMA1 hydrophobic cleft, which is a hotspot for targeting MJ complex formation. The proposed leads are the result of an exhaustive conformational search-based virtual screen with multilevel precision scoring of the docking affinities. These two compounds surpassed all the precision levels of docking and also the stringent post docking and cumulative molecular dynamics evaluations. Moreover, the backbone flexibility of hotspot residues in the hydrophobic cleft, which has been previously reported to be essential for accommodative binding of RON2 to AMA1, was also highly perturbed by these compounds. Furthermore, binding free energy calculations of these two compounds also revealed a significant affinity to AMA1. Machine learning approaches also predicted these two compounds to possess more relevant activities. Hence, these two leads, NSC95522 and NSC179676, may prove to be potential inhibitors targeting AMA1-RON2 complex formation towards combating toxoplasmosis.
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http://dx.doi.org/10.5808/GI.2016.14.2.53 | DOI Listing |
Int J Biol Macromol
December 2024
Department of Chemistry, Jashore University of Science and Technology, Jashore 7408, Bangladesh. Electronic address:
This study explores the interactions between pepsin and sodium dodecyl sulfate (SDS) using conductometric analysis and molecular docking to deepen our understanding of the role of pepsin. Conductometric studies were conducted to examine the micellization behavior of SDS in aqueous solutions of various sodium electrolytes (NaBr, Na₂SO₄, Na₃PO₄, and CH₃COONa) at temperatures ranging from 300.55 K to 320.
View Article and Find Full Text PDFACS Pharmacol Transl Sci
December 2024
Lab for Molecular Design & Pharm. Biophysics, Institute of Pharmaceutical Sciences, Eberhard Karls Universität Tübingen, 72076 Tübingen, Germany.
The tumor suppressor p53 is frequently mutated in human cancers. The Y220C mutant is the ninth most common p53 cancer mutant and is classified as a structural mutant, as it leads to strong thermal destabilization and degradation by creating a solvent-accessible hydrophobic cleft. To identify small molecules that thermally stabilize p53, we employed DSF to screen SAr-type electrophiles from our covalent fragment library (CovLib) for binding to different structural (Y220C, R282W) and DNA contact (R273H) mutants of p53.
View Article and Find Full Text PDFFront Mol Biosci
December 2024
Department of Chemistry, Western Washington University, Bellingham, WA, United States.
Cellular signaling networks are modulated by multiple protein-protein interaction domains that coordinate extracellular inputs and processes to regulate cellular processes. Several of these domains recognize short linear motifs, or SLiMs, which are often highly conserved and are closely regulated. One such domain, the Src homology 3 (SH3) domain, typically recognizes proline-rich SLiMs and is one of the most abundant SLiM-binding domains in the human proteome.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
Synthetic Biology Department, WuXi Biologics, 1951 Huifeng West Road, Fengxian District, Shanghai 201400, China. Electronic address:
J Chem Inf Model
December 2024
Department of Chemistry & Chemical Biology, Indian Institute of Technology (ISM) Dhanbad, Dhanbad 826004, India.
Since their inception in antibacterial therapy, macrolide-based antibiotics have significantly shaped the evolutionary pathways of pathogenic bacteria, driving them to develop diverse antimicrobial resistance (AMR) mechanisms. Among these, macrolide esterase, commonly referred to as erythromycin esterase, emerged as a critical defense mechanism, enabling bacteria to detoxify macrolides by hydrolyzing the macrolactone ring within the bacterial cell. In this study, we delve into the intricate interactions and conformational dynamics of erythromycin esterase C (EreC), a key member of the Ere enzyme family.
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