Effects of Calcium Ions on the Antimicrobial Activity of Gramicidin A

Fang, Shang-Ting; Huang, Shu-Hsiang; Yang, Chien-Wen; Liou, Je-Wen; Mani, Hemalatha; Chen, Yi-Cheng

doi:10.3390/biom12121799

Cited by 6 publications

(1 citation statement)

References 25 publications

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“…Gramicidin has been shown to bind to specific lipid components of the bacterial cell membrane, leading to the formation of ion channels and the influx of ions, which disrupts the membrane potential and leads to the loss of membrane integrity [97]. For example, gramicidin A (gA) forms a channel in lipid membranes, which allows H + ions conduction through the lipid bilayer of pathogens [98]. Surfactin also exhibits a range of antimicrobial mechanisms.…”

Section: B Mode Of Actionmentioning

confidence: 99%

Nature’s Antimicrobial Arsenal: Non-Ribosomal Peptides from PGPB for Plant Pathogen Biocontrol

et al. 2023

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Non-ribosomal peptides (NRPs) are a diverse group of bioactive compounds synthesized by microorganisms, and their antimicrobial properties make them ideal candidates for use as biocontrol agents against pathogens. Non-ribosomal peptides produced by Plant-Growth-Promoting Bacteria (PGPB) have gained interest for the biocontrol of plants’ bacterial and fungal pathogens. In this review, the structure and mode of action of NRPs, including their characterization and the characterization of NRP-producing microorganisms, are discussed. The use of NRPs in soilless agriculture and their potential as part of a sustainable plant disease control strategy are also highlighted. In addition, the review debates the commercial aspects of PGPB’s formulations and their potential as a biocontrol agent. Overall, this review emphasizes the importance of NRPs derived from PGPB in the biocontrol of plant pathogens and their potential to be used as an environmentally friendly and sustainable plant disease control strategy.

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Section: B Mode Of Actionmentioning

confidence: 99%

Nature’s Antimicrobial Arsenal: Non-Ribosomal Peptides from PGPB for Plant Pathogen Biocontrol

et al. 2023

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NMR structural studies of antimicrobial peptide, LPcin‐YK5, with divalent metal ion and its antimicrobial activity

Kim,

Park,

Kim

2024

Bulletin Korean Chem Soc

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Research studies on antimicrobial peptides (AMPs) that can combat antibiotic‐resistant bacteria, an issue with antibiotic usage, are garnering attention. Among the AMP types, cationic AMPs can electrostatically interact with the bacterial membrane and destroy it, resulting in bacterial death. In the presence of metal ions, these cationic AMPs possess beneficial antimicrobial activity. In the present study, through structural change analysis and antimicrobial activity tests, we elucidated whether LPcin‐YK5, a bovine‐derived AMP analog with enhanced antimicrobial activity, interacts with the divalent ions copper(II) and zinc(II) ions. We observed that the interaction between YK5 and divalent ions contributed to the secondary structure stability of YK5, resulting in a synergistic effect on the antimicrobial activity; this is consistent with the interaction between other cationic AMPs and divalent ions. Interestingly, the secondary structural changes and antimicrobial activity against gram‐negative bacteria of YK5 were more notable in the presence of zinc(II) than in that of copper(II). Therefore, the effects of YK5 and divalent ions may have implications for designing antibiotics against antibiotic‐resistant microorganisms.

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Monovalent cation binding to model systems and the macrocyclic depsipeptide, emodepside

Subramanian,

Manchanda,

et al. 2024

J Comput Chem

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This study focuses on the systematic exploration of the emodepside conformations bound to monovalent K+ ion using quantum mechanical density functional theory (DFT) calculations at the M06‐2X/6‐31+G(d,p) level of theory. Nine conformers of emodepside and their complexes with K+ ion were characterized as stationary points on the potential energy surface. The conformational isomers were examined for their 3D structures, bonding, energetics, and interactions with the cation. A cavitand‐like structure (CC) is identified to be the energetically most stable arrangement. To arrive at a better understanding of the K+ ion binding, calculations were initially performed on complexes formed by the K+ and Na+ ions with model ligands (methyl ester and N,N‐dimethyl acetamide). Both the natural bond orbital (NBO) method and the block‐localized wavefunction (BLW) energy decomposition approach was employed to assess the bonding and energetic contributions stabilizing the ion‐bound model complexes. Finally, the solvent effect was evaluated through complete geometry optimizations and energy minimizations for the model ion‐ligand complexes and the emodepside‐K+ bound complexes using an implicit solvent model mimicking water and DMSO.

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Effects of Calcium Ions on the Antimicrobial Activity of Gramicidin A

Cited by 6 publications

References 25 publications

Nature’s Antimicrobial Arsenal: Non-Ribosomal Peptides from PGPB for Plant Pathogen Biocontrol

Nature’s Antimicrobial Arsenal: Non-Ribosomal Peptides from PGPB for Plant Pathogen Biocontrol

NMR structural studies of antimicrobial peptide, LPcin‐YK5, with divalent metal ion and its antimicrobial activity

Monovalent cation binding to model systems and the macrocyclic depsipeptide, emodepside

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