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http://dx.doi.org/10.1001/jamaophthalmol.2024.4377 | DOI Listing |
Soft comput
July 2024
Computer Science and Engineering, KL University, Guntur, Andra Pradesh India.
[This retracts the article DOI: 10.1007/s00500-022-06943-x.].
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August 2024
Department of Computer Science and Engineering, GITAM School of Technology, GITAM University, Bengaluru, India.
[This retracts the article DOI: 10.1007/s00500-023-08313-7.].
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July 2024
eVIDA Lab, The University of Deusto, Avda/Universidades 24, Bilbao, 48007 Spain.
[This retracts the article DOI: 10.1007/s00500-020-05424-3.].
View Article and Find Full Text PDFJ Phys Chem B
January 2025
Research Center for Analytical Sciences, Tianjin Key Laboratory of Biosensing and Molecular Recognition, State Key Laboratory of Medicinal Chemical, Biology College of Chemistry, Nankai University, Tianjin 300071, China.
PGLa, an antimicrobial peptide (AMP), primarily exerts its antibacterial effects by disrupting bacterial cell membrane integrity. Previous theoretical studies mainly focused on the binding mechanism of PGLa with membranes, while the mechanism of water pore formation induced by PGLa peptides, especially the role of structural flexibility in the process, remains unclear. In this study, using all-atom simulations, we investigated the entire process of membrane deformation caused by the interaction of PGLa with an anionic cell membrane composed of dimyristoylphosphatidylcholine (DMPC) and dimyristoylphosphatidylglycerol (DMPG).
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