biostudies-literatureUnknown20(9)Hossain MMOne of the most crucial respiratory pathogens in the world, namely human metapneumovirus (HMPV), causes acute upper and lower respiratory tract infection. The HMPV Fusion (F) protein is a vital element for viral entry and is the sole target of neutralizing antibodies, making it a prime target for drug and vaccine development. Targeting the Fusion (F) protein of HMPV for inhibition has emerged as a potential therapeutic strategy, particularly in respiratory infection treatment. We aimed to identify potential inhibitors against HMPV F protein by molecular docking and molecular dynamics study. Through molecular docking, we were able to identify 16 lead compounds derived from Dolichos lablab (DL). These compounds exhibited robust binding affinities with the HMPV F protein, with better docking PloS onee0332170https://www.ebi.ac.uk/biostudies/studies/S-EPMC12425334biostudies-literatureExploring Dolichos lablab compounds as potential inhibitors for fusion (F) protein of human metapneumovirus (HMPV): A systematic computational approach.PMC12425334Kar ADas LCApu MJHHossain MMMorshed MMAziz MFBATanjil MTREvamoni FZfalseExploring Dolichos lablab compounds as potential inhibitors for fusion (F) protein of human metapneumovirus (HMPV): A systematic computational approach.One of the most crucial respiratory pathogens in the world, namely human metapneumovirus (HMPV), causes acute upper and lower respiratory tract infection. The HMPV Fusion (F) protein is a vital element for viral entry and is the sole target of neutralizing antibodies, making it a prime target for drug and vaccine development. Targeting the Fusion (F) protein of HMPV for inhibition has emerged as a potential therapeutic strategy, particularly in respiratory infection treatment. We aimed to identify potential inhibitors against HMPV F protein by molecular docking and molecular dynamics study. Through molecular docking, we were able to identify 16 lead compounds derived from Dolichos lablab (DL). These compounds exhibited robust binding affinities with the HMPV F protein, with better docking 2025-01-01T00:00:00Z20252026-06-03T02:24:07.768Z2026-04-23T03:09:55.628ZS-EPMC124253344093424410.1371/journal.pone.0332170