ArticlePloS one2017
Computational study of aggregation mechanism in human lysozyme[D67H].
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Effects of dietary lysozyme supplementation on growth performance, intestinal morphology, immune function, antioxidant capacity, and gut microbiota in broilers.Poultry science · 2025Article
- Paired Simulations and Experimental Investigations into the Calcium-Dependent Conformation of Albumin.Journal of chemical information and modeling · 2022Article
- Probing protein aggregation at buried interfaces: distinguishing between adsorbed protein monomers, dimers, and a monomer-dimer mixtureChemical science · 2022Article
- Article
- Comparison of the pH- and thermally-induced fluctuations of a therapeutic antibody Fab fragment by molecular dynamics simulation.Computational and structural biotechnology journal · 2021Article
- Dietary Lysozyme Alters Sow's Gut Microbiota, Serum Immunity and Milk Metabolite Profile.Frontiers in microbiology · 2019Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aggregation of proteins is an undesired phenomena that affects both human health and bioengineered products such as therapeutic proteins. Finding preventative measures could be facilitated by a molecular-level understanding of dimer formation, which is the first step in aggregation. Here we present a molecular dynamics (MD) study of dimer formation propensity in human lysozyme and its D67H variant. Because the latter protein aggregates while the former does not, they offer an ideal system for testing the feasibility of the proposed MD approach which comprises three stages: i) partially unfolded conformers involved in dimer formation are generated via high-temperature MD simulations, ii) potential dimer structures are searched using docking and refined with MD, iii) free energy calculations are performed to find the most stable dimer structure. Our results provide a detailed explanation for how a single mutation (D67H) turns human lysozyme from non-aggregating to an aggregating protein. Conversely, the proposed method can be used to identify the residues causing aggregation in a protein, which can be mutated to prevent it.
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Registered trials
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