ArticleBiochimica et biophysica acta2006
Driving engineering of novel antimicrobial peptides from simulations of peptide-micelle interactions.
Article in Biochimica et biophysica acta, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Activatable prodrug for controlled release of an antimicrobial peptide via the proteases overexpressed inTheranostics · 2024Article
- Conformation and membrane interaction studies of the potent antimicrobial and anticancer peptide palustrin-Ca.Scientific reports · 2021Article
- Effect of monovalent salt concentration and peptide secondary structure in peptide-micelle binding.RSC advances · 2021Article
- Molecular Dynamics Simulations of Human Antimicrobial Peptide LL-37 in Model POPC and POPG Lipid Bilayers.International journal of molecular sciences · 2018Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Beyond histograms: efficiently estimating radial distribution functions via spectral Monte Carlo.The Journal of chemical physics · 2017Article
- pMPES: A Modular Peptide Expression System for the Delivery of Antimicrobial Peptides to the Site of Gastrointestinal Infections Using Probiotics.Pharmaceuticals (Basel, Switzerland) · 2016Article
- Multiscale Models of Antibiotic Probiotics.Current opinion in chemical engineering · 2014Article
- Binding to the lipid monolayer induces conformational transition in Aβ monomer.Journal of molecular modeling · 2013Article
- Multiscale models of the antimicrobial peptide protegrin-1 on gram-negative bacteria membranes.International journal of molecular sciences · 2012Review
- Thermodynamic analysis of protegrin-1 insertion and permeation through a lipid bilayer.The journal of physical chemistry. B · 2011Article
- Review
- Dimerization of protegrin-1 in different environments.International journal of molecular sciences · 2010Article
- Antimicrobial mechanism of pore-forming protegrin peptides: 100 pores to kill E. coli.Peptides · 2010Article
- Relative free energy of binding between antimicrobial peptides and SDS or DPC micelles.Molecular simulation · 2009Article
- Article
- On the nature of antimicrobial activity: a model for protegrin-1 pores.Journal of the American Chemical Society · 2008Article
- Interactions of cationic-hydrophobic peptides with lipid bilayers: a Monte Carlo simulation method.Biophysical journal · 2007Article
- Molecular dynamics simulations of three protegrin-type antimicrobial peptides: interplay between charges at the termini, β-sheet structure and amphiphilic interactions.Molecular simulation · 2007Article
- Comparison of interactions between beta-hairpin decapeptides and SDS/DPC micelles from experimental and simulation data.BMC biochemistry · 2007Article
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Authors and funding
3 authors.
Funding
Abstract
Simulations of antimicrobial peptides in membrane mimics can provide the high resolution, atomistic picture that is necessary to decipher which sequence and structure components are responsible for activity and toxicity. With such detailed insight, engineering new sequences that are active but non-toxic can, in principle, be rationalized. Armed with supercomputers and accurate force fields for biomolecular interactions, we can now investigate phenomena that span hundreds of nanoseconds. Although the phenomena involved in antimicrobial activity, (i.e., diffusion of peptides, interaction with lipid layers, secondary structure attainment, possible surface aggregation, possible formation of pores, and destruction of the lipid layer integrity) collectively span time scales still prohibitively long for classical mechanics simulations, it is now feasible to investigate the initial approach of single peptides and their interaction with membrane mimics. In this article, we discuss the promise and the challenges of widely used models and detail our recent work on peptide-micelle simulations as an attractive alternative to peptide-bilayer simulations. We detail our results with two large structural classes of peptides, helical and beta-sheet and demonstrate how simulations can assist in engineering of novel antimicrobials with therapeutic potential.
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