ArticleThe journal of physical chemistry. B2011
Thermodynamic analysis of protegrin-1 insertion and permeation through a lipid bilayer.
Article in The journal of physical chemistry. B, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 25 citations in OpenAlex.
- Thermodynamics and Mechanism of the Membrane Permeation of Hv1 Channel Blockers.The Journal of membrane biology · 2021Article
- Interactions of GF-17 derived from LL-37 antimicrobial peptide with bacterial membranes: a molecular dynamics simulation study.Journal of computer-aided molecular design · 2020Article
- Transmembrane Pore Structures of β-Hairpin Antimicrobial Peptides by All-Atom Simulations.The journal of physical chemistry. B · 2017Article
- Computational studies of peptide-induced membrane pore formation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Computational prediction of the optimal oligomeric state for membrane-inserted β-barrels of protegrin-1 and related mutants.Journal of peptide science : an official publication of the European Peptide Society · 2017Article
- Implicit Membrane Investigation of the Stability of Antimicrobial Peptide β-Barrels and Arcs.The Journal of membrane biology · 2015Article
- Implicit membrane treatment of buried charged groups: application to peptide translocation across lipid bilayers.Biochimica et biophysica acta · 2014Article
- Membrane interactions and pore formation by the antimicrobial peptide protegrin.Biophysical journal · 2013Article
- Amphiphilic adsorption of human islet amyloid polypeptide aggregates to lipid/aqueous interfaces.Journal of molecular biology · 2012Article
- Multiscale models of the antimicrobial peptide protegrin-1 on gram-negative bacteria membranes.International journal of molecular sciences · 2012Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Molecular dynamics (MD) simulations are used to study the pathway for the insertion of the cationic antimicrobial peptide protegrin-1 (PG1) into mixed anionic lipid bilayers composed of palmitoyl-oleoyl-phosphatidylglycerol (POPG) and palmitoyl-oleoyl-phosphatidylethanolamine (POPE) in a 1:3 ratio (POPG/POPE). We calculate the potential of mean force (PMF) during the transfer of the peptide from the bulk aqueous phase to the transmembrane (TM) configuration using the adaptive biasing force (ABF) method. We find that the PMF has two energy minima separated by an energy barrier. One minimum corresponds to the fully transmembrane inserted state, with a free energy of -20.1 kcal/mol. The second PMF minimum, which corresponds to adsorption to the membrane surface, has a value of -2.5 kcal/mol. The PMF also shows the existence of a free energy barrier of +6.3 kcal/mol for the insertion process. Using the Kramers theory Langevin equation and the Grote-Hynes theory generalized Langevin equation, we calculated the transmission coefficient for PG1 diffusion through the potential barrier. We focus on the use of the PMF and the time correlation function of the fluctuation of the instantaneous force to calculate the rate constants for insertion/deinsertion of PG1 from the mixed POPG/POPE membrane. The influence of the activation free energy barrier on the dynamics of the insertion and permeation of peptides through the membrane are discussed.
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Registered trials
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