ArticleComputational and structural biotechnology journal2026
Theta-Defensin Proteins: Conformational Variability and Environmental Effects.
Article in Computational and structural biotechnology journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Authors and funding
4 authors.
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Abstract
Theta-defensins are a unique class of cyclic antimicrobial peptides known for their exceptional structural stability and broad-spectrum antimicrobial activity. Despite their therapeutic potential in mammals, the effects of solvent environments and specific mutations on their conformational stability remain poorly understood. This paper employs all-atom molecular dynamics simulations under different solvent conditions to investigate the structural dynamics of baboon theta-defensin-2 (BTD-2) peptides, as well as solvent effects. BTD-2 was selected due to its higher arginine content, enhancing its antimicrobial potency compared to that of the rhesus theta-defensin-1 protein. We compare the dynamics of 3 different BTD-2 conformations and assess their flexibility, residual fluctuations, and thermal stability. Although similar in sequence, these peptides provide conformation-specific temporal characteristics. The insights gained through the analysis of the simulation data contribute to a deeper understanding of theta-defensin stability, providing important information related to the rational design of peptide-based antimicrobial and antiviral therapeutics.
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Registered trials
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