Biophysical and in-silico studies on the structure-function relationship of Brugia malayi protein disulfide isomerase

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dc.contributor.authorDoharey P.K.
dc.contributor.authorVerma P.
dc.contributor.authorDubey A.
dc.contributor.authorSingh S.K.
dc.contributor.authorKumar M.
dc.contributor.authorTripathi T.
dc.contributor.authorAlonazi M.
dc.contributor.authorSiddiqi N.J.
dc.contributor.authorSharma B.
dc.date.accessioned2025-01-13T07:09:28Z
dc.date.available2025-01-13T07:09:28Z
dc.date.issued2024
dc.description.abstractHuman Lymphatic filariasis is caused by parasitic nematodes Wuchereria bancrofti, Brugia malayi, and Brugia timori. Protein disulfide isomerase (PDI), a redox-active enzyme, helps to form and isomerize the disulfide bonds, thereby acting as a chaperone. Such activity is essential for activating many essential enzymes and functional proteins. Brugia malayi protein disulfide isomerase (BmPDI) is crucial for parasite survival and an important drug target. Here, we used a combination of spectroscopic and computational analysis to study the structural and functional changes in the BmPDI during unfolding. Tryptophan fluorescence data revealed two well-separated transitions during the unfolding process, suggesting that the unfolding of the BmPDI is non-cooperative. The binding of the fluorescence probe 8-anilino-1-naphthalene sulfonic acid dye (ANS) validated the results obtained by the pH unfolding. The dynamics of molecular simulation performed at different pH conditions revealed the structural basis of BmPDI unfolding. Detailed analysis suggested that under different pH, both the global structure and the conformational dynamics of the active site residues were differentially altered. Our multiparametric study reveals the differential dynamics and collective motions of BmPDI unfolding, providing insights into its structure-function relationship. Communicated by Ramaswamy H. Sarma. � 2023 Informa UK Limited, trading as Taylor & Francis Group.
dc.identifier.doi10.1080/07391102.2023.2201849
dc.identifier.issn7391102
dc.identifier.urihttps://dl.bhu.ac.in/ir/handle/123456789/3700
dc.language.isoen
dc.publisherTaylor and Francis Ltd.
dc.subjectBrugia malayi protein disulfide isomerase
dc.subjectmolecular dynamics
dc.subjectpH
dc.subjectprotein-unfolding
dc.subjecturea and guanidine hydrochloride
dc.titleBiophysical and in-silico studies on the structure-function relationship of Brugia malayi protein disulfide isomerase
dc.typeArticle
journal.titleJournal of Biomolecular Structure and Dynamics
journalvolume.identifier.volume42

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