Molecular docking studies on the interaction of the Cryptosporidium parvum proteins, lactate dehydrogenase (LDH) and calcium-dependent protein kinase-1 (CpCDPK1), with selected plant compounds
Date of Publication
2024
Document Type
Bachelor's Thesis
Degree Name
Bachelor of Science in Biology major in Medical Biology
Subject Categories
Biology
College
College of Science
Department/Unit
Biology
Thesis Advisor
Frances C. Recuenco
Defense Panel Chair
Thaddeus M. Carvajal
Defense Panel Member
Searle Aichelle S. Duay
Raymond Vincent F. Castillo
Abstract/Summary
Lactate dehydrogenase (LDH) and calcium-dependent protein kinase-1 (CpCDPK1) are proteins involved in the life cycle and pathogenicity of Cryptosporidium parvum, the protozoan parasite that causes waterborne gastrointestinal disease in humans and animals. LDH is for the energy production of the parasite especially during its sporozoite and merozoite life stages while CpCDPK1 is for the regulation of invasion, egress, and development. Aloe vera, Ehretia microphylla, Blumea balsamifera, Zingiber officinale, and Thymus vulgaris are plants that have been used in folk medicine due to their antimicrobial properties. In this study, an in silico approach was used to predict the interactions between compounds from these plants against the LDH and CpCDPK1 proteins. Molecular dynamics RMSD analysis and molecular docking were performed. First, the structures of the proteins and ligands were obtained from RCSB Protein Data Bank and PubChem. Then, the stable conformations of the proteins before docking were predicted using COARE and Gromacs-2023.3. Prior to docking, the RMSD graphs confirmed the stabilization of the proteins at 40000 ns. To obtain the predicted binding affinities, Autodock Vina was used. Consequently, Discovery Studio Visualizer was utilized to visualize the predicted interactions. Ehretianone from E. microphylla and aloin from A. vera are predicted to have the strongest binding affinities with LDH (-7.8 kcal/mol) and CpCDPK1 (-8.6 kcal/mol). The predicted interactions involved among all the ligands are van der Waals, conventional hydrogen bonds, carbon-hydrogen bonds, alkyl and pi-alkyl bonds, pi-sigma bonds, pi-pi T-shaped bonds, pi-cation bonds, pi-anion bonds, amide-pi stacked bonds, and unfavorable acceptors and donor bonds. These predicted interactions may be useful in considering the plant sources for their potential as anti-cryptosporidial drugs. In vitro and in vivo studies must be conducted to establish a better understanding of these interactions.
Abstract Format
html
Language
English
Format
Electronic
Keywords
Cryptosporidium parvum; Lactate dehydrogenase
Recommended Citation
Samson, I. O., & Quijano, R. C. (2024). Molecular docking studies on the interaction of the Cryptosporidium parvum proteins, lactate dehydrogenase (LDH) and calcium-dependent protein kinase-1 (CpCDPK1), with selected plant compounds. Retrieved from https://animorepository.dlsu.edu.ph/etdb_bio/59
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Embargo Period
4-16-2024