ArticleMolecules (Basel, Switzerland)2017
Molecular Dynamics Simulations of the Host Defense Peptide Temporin L and Its Q3K Derivative: An Atomic Level View from Aggregation in Water to Bilayer Perturbation.
Article in Molecules (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Mechanistic Insights into the Membrane Permeabilization Activity of Antimicrobial Prenylated Isoflavonoids: A Comparative Study of Glabridin, Wighteone, and Lupiwighteone.Journal of agricultural and food chemistry · 2025Article
- In silico and physico-chemical characterization of cluster formation dynamics in peptide solutions.Biochemistry and biophysics reports · 2024Article
- Insights into the Binding Mode of Lipid A to the Anti-lipopolysaccharide Factor ALFPm3 fromJournal of chemical information and modeling · 2023Article
- Review
- Fighting Against Bacterial Lipopolysaccharide-Caused Infections through Molecular Dynamics Simulations: A Review.Journal of chemical information and modeling · 2021Review
- Activity of Anti-Microbial Peptides (AMPs) againstBiomolecules · 2021Review
- Aggregation and Its Influence on the Bioactivities of a Novel Antimicrobial Peptide, Temporin-PF, and Its Analogues.International journal of molecular sciences · 2021Article
- Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities.Scientific reports · 2019Article
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Authors and funding
7 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Temporin L (TempL) is a 13 residue Host Defense Peptide (HDP) isolated from the skin of frogs. It has a strong affinity for lipopolysaccharides (LPS), which is related to its high activity against Gram-negative bacteria and also to its strong tendency to neutralize the pro-inflammatory response caused by LPS release from inactivated bacteria. A designed analog with the Q3K substitution shows an enhancement in both these activities. In the present paper, Molecular Dynamics (MD) simulations have been used to investigate the origin of these improved properties. To this end, we have studied the behavior of the peptides both in water solution and in the presence of LPS lipid-A bilayers, demonstrating that the main effect through which the Q3K substitution improves the peptide activities is the destabilization of peptide aggregates in water.
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