ArticleBiophysical journal2009
Comparative molecular dynamics simulation studies of protegrin-1 monomer and dimer in two different lipid bilayers.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Experimental and Computational Characterization of Oxidized and Reduced Protegrin Pores in Lipid Bilayers.The Journal of membrane biology · 2020Article
- Transmembrane Pore Structures of β-Hairpin Antimicrobial Peptides by All-Atom Simulations.The journal of physical chemistry. B · 2017Article
- 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
- Refinement of OprH-LPS Interactions by Molecular Simulations.Biophysical journal · 2017Article
- Implicit Membrane Investigation of the Stability of Antimicrobial Peptide β-Barrels and Arcs.The Journal of membrane biology · 2015Article
- Solid-State NMR-Restrained Ensemble Dynamics of a Membrane Protein in Explicit Membranes.Biophysical journal · 2015Article
- Expression of porcine protegrin-1 inExperimental and therapeutic medicine · 2015Article
- E. coli outer membrane and interactions with OmpLA.Biophysical journal · 2014Article
- NMR-based simulation studies of Pf1 coat protein in explicit membranes.Biophysical journal · 2013Article
- Article
- Membrane interactions and pore formation by the antimicrobial peptide protegrin.Biophysical journal · 2013Article
- Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Antimicrobial peptides interact specifically with the membrane of a pathogen and kill the pathogen by releasing its cellular contents. Protegrin-1 (PG-1), a beta-hairpin antimicrobial peptide, is known to exist as a transmembrane monomer in a 1,2-dilauroylphosphatidylcholine (DLPC) bilayer and shows concentration-dependent oligomerization in a 1-palmitoyl-2-oleoylphosphatidylcholine (POPC) bilayer. To examine its structure, dynamics, orientation, and interaction in membranes, we performed comparative molecular dynamics simulations of PG-1 monomer and dimer in DLPC and POPC bilayers for a total of 840 ns. The PG-1 monomer exhibits larger tilting in DLPC than in POPC due to a hydrophobic mismatch. PG-1 tilting is dependent on its rotation angle. The specific orientation of PG-1 in membranes is governed by the interactions of its aromatic residues with lipid headgroups. The calculated (15)N and (13)CO chemical shifts of Val(16) in DLPC reveal that there are different sets of tilt and rotation angles that satisfy the experimental values reasonably, suggesting that more experiments are needed to determine its orientation. The dimer simulations show that the dimer interface is better preserved in POPC than in DLPC because POPC's greater hydrophobic thickness causes reduced flexibility of the C-terminal strands. Both monomer and dimer simulations show membrane thinning around PG-1, largely due to arginine-lipid interactions.
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