ResearchArticle Molecular Modeling Identification of Key Secondary Metabolites from Xylopia aethiopica as Promising Therapeutics Targeting Essential Measles Viral Proteins Jeremiah John Oloche , 1,2 Bolaji Bosede Oluremi, 3 Christiana Eleojo Aruwa , 4 and Saheed Sabiu 4 1 Department of Pharmacology and Terapeutics, College of Health Sciences, Benue State University of Makurdi, Makurdi, Nigeria 2 Department of Pharmacology and Terapeutics, College of Medicine, University of Ibadan, Oyo State, Ibadan, Nigeria 3 Department of Pharmaceutical Microbiology, University of Ibadan, Oyo State, Ibadan, Nigeria 4 Department of Biotechnology and Food Science, Faculty of Applied Sciences, Durban University of Technology, Durban, South Africa Correspondence should be addressed to Saheed Sabiu; sabius@dut.ac.za Received 22 September 2022; Revised 7 November 2022; Accepted 24 January 2023; Published 9 February 2023 Academic Editor: Xuezhong Zhou Copyright © 2023 Jeremiah John Oloche et al. Tis is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Tis study computationally screened three key compounds (vanillin (VAN), oxophoebine (OPB), and dihydrochalcone (DHC)) derived from Xylopiaaethiopica (Guinea pepper), a medicinal plant with known antiviral activity, against key druggable measles virus (MV) proteins (fusion protein (FUP), haemagglutinin protein (HMG), and phosphoprotein (PSP)). Each molecular species was subjected to a 100 ns molecular dynamics (MD) simulation following docking, and a range of postdynamic parameters including free binding energy and pharmacokinetic properties were determined. Te docking scores of the resulting OPB•FUP (−5.4 kcal/mol), OPB•HMG (−8.1kcal/mol), and OPB•PSP (−8.0 kcal/mol) complexes were consistent with their respective binding energy values (−25.37, −28.74, and −40.68 kcal/mol), and higher than that of the reference standard, ribavirin (RBV) in each case. Furthermore, all the investigated compounds were thermodynamically compact and stable, especially HMG of MV, and this observation could be attributed to the resulting intermolecular interactions in each system. Overall, OPB may possess inhibitory properties against MV glycoproteins (FUP and HMG) and PSP that play important roles in the replication of MV and measles pathogenesis. hile OPB could serve as a scafold for the development of novel MV fusion and entry inhibitors, further in vitro and invivo evaluation is highly recommended. 1. Introduction Measles is a communicable disease caused by a member of the genus Morbillivirus, and species Measles morbillivirus, also referred to as the measles virus (MV) [1, 2]. Te measles virus infects the central nervous system leading to serious neurological disorders. Despite the availability of clinically efective live attenuated vaccines currently in use, the disease is one the major cause of morbidity and mortality largely among unvaccinated children. Te disease accounted for approximately 140,000 global deaths in children below 5 years in 2018, with most of the reported cases occurring in Africa and the Eastern Mediterranean regions [3]. Recently, over a thousand children were reportedly infected in a measles outbreak in North•East Nigeria [4]. Te measles virus is an enveloped antigenically monotypic negative•sensesingle•stranded RNA virus [5]. Te measles virus core consists of an RNA genome covered by a nucleocapsid protein that is surrounded by an envelope composed of glyco• proteins such as haemagglutinin ( H) and fusion ( F) proteins [6]. Te pathogenesis of measles virus infection is highly coordinated and involves an initial binding of H protein Hindawi Evidence-Based Complementary and Alternative Medicine Volume 2023, Article ID 1575358, 13 pages https://doi.org/10.1155/2023/1575358