Insights into Membrane Translocation of Protegrin Antimicrobial Peptides by Multistep Molecular Dynamics Simulations.

scientific article

Insights into Membrane Translocation of Protegrin Antimicrobial Peptides by Multistep Molecular Dynamics Simulations. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1021/ACSOMEGA.8B00483
P932PMC publication ID6026836
P698PubMed publication ID29978143

P50authorYiannis N. KaznessisQ57101215
Pin-Kuang LaiQ86487920
P2093author name stringYiannis N. Kaznessis
P2860cites workComputational electrophysiology: the molecular dynamics of ion channel permeation and selectivity in atomistic detailQ24635944
On the nature of antimicrobial activity: a model for protegrin-1 poresQ24657144
CHARMM: the biomolecular simulation programQ24658108
Ion leakage through transient water pores in protein-free lipid membranes driven by transmembrane ionic charge imbalanceQ24675686
Cationic membrane peptides: atomic-level insight of structure-activity relationships from solid-state NMRQ26830018
Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytesQ27733422
Antimicrobial peptides of multicellular organismsQ28131811
Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?Q29547675
Update of the CHARMM all-atom additive force field for lipids: validation on six lipid typesQ29616710
Computational prediction of the optimal oligomeric state for membrane-inserted β-barrels of protegrin-1 and related mutantsQ30152643
Implicit Membrane Investigation of the Stability of Antimicrobial Peptide β-Barrels and ArcsQ30153294
Membrane-dependent oligomeric structure and pore formation of a beta-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR.Q30159595
Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranesQ30482157
Solid-state NMR investigations of peptide-lipid interaction and orientation of a beta-sheet antimicrobial peptide, protegrinQ30839725
Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR.Q31122049
Antimicrobial mechanism of pore-forming protegrin peptides: 100 pores to kill E. coliQ33674830
CHARMM-GUI Membrane Builder toward realistic biological membrane simulationsQ34195752
Computational studies of protegrin antimicrobial peptides: a review.Q34455757
A lipocentric view of peptide-induced pores.Q34757093
Protegrin-1: a broad-spectrum, rapidly microbicidal peptide with in vivo activity.Q35137651
Adaptive translocation: the role of hydrogen bonding and membrane potential in the uptake of guanidinium-rich transporters into cellsQ36049543
Arginine in α-defensins: differential effects on bactericidal activity correspond to geometry of membrane curvature generation and peptide-lipid phase behavior.Q36052424
APD3: the antimicrobial peptide database as a tool for research and educationQ36434966
CHARMM-GUI Input Generator for NAMD, GROMACS, AMBER, OpenMM, and CHARMM/OpenMM Simulations Using the CHARMM36 Additive Force FieldQ36461179
Guanidinium group: a versatile moiety inducing transport and multicompartmentalization in complementary membranesQ37051795
110 years of the Meyer-Overton rule: predicting membrane permeability of gases and other small compoundsQ37513966
Defect-mediated trafficking across cell membranes: insights from in silico modelingQ37778373
Computational studies of peptide-induced membrane pore formationQ38669154
A molecular insight into the electro-transfer of small molecules through electropores driven by electric fieldsQ38790614
Antimicrobial Peptides Share a Common Interaction Driven by Membrane Line Tension Reduction.Q39183260
Phosphatidylethanolamine-phosphatidylglycerol bilayer as a model of the inner bacterial membraneQ40315778
APD: the Antimicrobial Peptide DatabaseQ40403120
Antimicrobial Peptide Simulations and the Influence of Force Field on the Free Energy for Pore Formation in Lipid BilayersQ40574291
High-yield nontoxic gene transfer through conjugation of the CM₁₈-Tat₁₁ chimeric peptide with nanosecond electric pulses.Q42662499
APD2: the updated antimicrobial peptide database and its application in peptide designQ43122430
Role of membrane potential and hydrogen bonding in the mechanism of translocation of guanidinium-rich peptides into cellsQ45005329
Toroidal pores formed by antimicrobial peptides show significant disorder.Q46500589
Transmembrane Pore Structures of β-Hairpin Antimicrobial Peptides by All-Atom Simulations.Q47896925
Atomistic Molecular Simulations Suggest a Kinetic Model for Membrane Translocation by Arginine-Rich Peptides.Q50788764
Atomistic simulations of biologically realistic transmembrane potential gradients.Q51980908
Electroporation of heterogeneous lipid membranes.Q54719809
Membrane-bound dimer structure of a beta-hairpin antimicrobial peptide from rotational-echo double-resonance solid-state NMRQ57099586
Transport of siRNA through Lipid Membranes Driven by Nanosecond Electric Pulses: An Experimental and Computational StudyQ60313921
Molecular Mechanism for Lipid Flip-FlopsQ61875084
Molecular electroporation: a unifying concept for the description of membrane pore formation by antibacterial peptides, exemplified with NK-lysinQ73224026
Polyarginine enters cells more efficiently than other polycationic homopolymersQ73233590
Action of antimicrobial peptides: two-state modelQ74061744
Antimicrobial peptides in actionQ80248535
Lipids out of equilibrium: energetics of desorption and pore mediated flip-flopQ80290054
CHARMM-GUI: a web-based graphical user interface for CHARMMQ80900573
P433issue6
P921main subjectantimicrobial peptideQ1201508
P304page(s)6056-6065
P577publication date2018-06-05
P1433published inACS OmegaQ27727647
P1476titleInsights into Membrane Translocation of Protegrin Antimicrobial Peptides by Multistep Molecular Dynamics Simulations
P478volume3

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cites work (P2860)
Q92642351Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria
Q92534860Protegrin-1 cytotoxicity towards mammalian cells positively correlates with the magnitude of conformational changes of the unfolded form upon cell interaction

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