{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chakraborty A"],"funding":["University of Auckland","Royal Society of New Zealand","Commonwealth Scholarship Commission"],"pagination":["388-400"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7807746"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["6(1)"],"pubmed_abstract":["Antimicrobial peptides (AMPs) are a potential solution to the increasing threat of antibiotic resistance, but successful design of active but nontoxic AMPs requires understanding their mechanism of action. Molecular dynamics (MD) simulations can provide atomic-level information regarding how AMPs interact with the cell membrane. Here, we have used MD simulations to study two linear analogs of battacin, a naturally occurring cyclic, lipidated, nonribosomal AMP. Like battacin, these analogs are active against Gram-negative multidrug resistant and Gram-positive bacteria, but they are less toxic than battacin. Our simulations show that this activity depends upon a combination of positively charged and hydrophobic moieties. Favorable interactions with negatively charged membrane lipid head groups drive association with the membrane and insertion of hydrophobic residues, and the N-terminal lipid anchors the peptides to the membrane surface. Both effects are required for stable membrane binding."],"journal":["ACS omega"],"pubmed_title":["Molecular Dynamics Simulation of the Interaction of Two Linear Battacin Analogs with Model Gram-Positive and Gram-Negative Bacterial Cell Membranes."],"pmcid":["PMC7807746"],"funding_grant_id":["15-MAU-001"],"pubmed_authors":["Allison JR","Chan J","de Zoysa GH","Chakraborty A","Piggot TJ","Kobzev E","Sarojini V"],"additional_accession":[]},"is_claimable":false,"name":"Molecular Dynamics Simulation of the Interaction of Two Linear Battacin Analogs with Model Gram-Positive and Gram-Negative Bacterial Cell Membranes.","description":"Antimicrobial peptides (AMPs) are a potential solution to the increasing threat of antibiotic resistance, but successful design of active but nontoxic AMPs requires understanding their mechanism of action. Molecular dynamics (MD) simulations can provide atomic-level information regarding how AMPs interact with the cell membrane. Here, we have used MD simulations to study two linear analogs of battacin, a naturally occurring cyclic, lipidated, nonribosomal AMP. Like battacin, these analogs are active against Gram-negative multidrug resistant and Gram-positive bacteria, but they are less toxic than battacin. Our simulations show that this activity depends upon a combination of positively charged and hydrophobic moieties. Favorable interactions with negatively charged membrane lipid head groups drive association with the membrane and insertion of hydrophobic residues, and the N-terminal lipid anchors the peptides to the membrane surface. Both effects are required for stable membrane binding.","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Jan","modification":"2024-02-15T07:25:24.402Z","creation":"2021-02-20T23:27:28Z"},"accession":"S-EPMC7807746","cross_references":{"pubmed":["33458490"],"doi":["10.1021/acsomega.0c04752"]}}