ArticleJournal of structural biology2009
Phospholipid flip-flop modulated by transmembrane peptides WALP and melittin.
Article in Journal of structural biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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Who cites it
18 citing papers in PubMed.
- Structural basis of closed groove scrambling by a TMEM16 protein.Nature structural & molecular biology · 2024Article
- Structural basis of closed groove scrambling by a TMEM16 protein.Research square · 2023Article
- Accelerating Lipid Flip-Flop at Low Concentrations: A General Mechanism for Membrane Binding Peptides.The journal of physical chemistry letters · 2023Article
- Molecular Transport and Growth of Lipid Vesicles Exposed to Antimicrobial Peptides.Langmuir : the ACS journal of surfaces and colloids · 2022Article
- Theoretical and experimental comparisons of simple peptide-membrane systems; towards defining the reaction space: general discussion.Faraday discussions · 2021Article
- Antimicrobial peptide activity in asymmetric bacterial membrane mimics.Faraday discussions · 2021Article
- A Diazirine-Modified Membrane Lipid to Study Peptide/Lipid Interactions - Chances and Challenges.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Gramicidin Increases Lipid Flip-Flop in Symmetric and Asymmetric Lipid Vesicles.Biophysical journal · 2019Article
- Enhanced Sampling of Coarse-Grained Transmembrane-Peptide Structure Formation from Hydrogen-Bond Replica Exchange.The Journal of membrane biology · 2015Article
- Production of antibacterial peptide from bee venom via a new strategy for heterologous expression.Molecular biology reports · 2014Article
- α-Synuclein-induced membrane remodeling is driven by binding affinity, partition depth, and interleaflet order asymmetry.Journal of the American Chemical Society · 2014Article
- Dependence of Alamethicin Membrane Orientation on the Solution Concentration.The journal of physical chemistry. C, Nanomaterials and interfaces · 2013Article
- Protein-phospholipid interactions in nonclassical protein secretion: problem and methods of study.International journal of molecular sciences · 2013Article
- Elucidation of molecular structures at buried polymer interfaces and biological interfaces using sum frequency generation vibrational spectroscopy.Soft matter · 2013Article
- Molecular interactions between cell penetrating peptide Pep-1 and model cell membranes.The journal of physical chemistry. B · 2012Article
- Molecular interactions of proteins and peptides at interfaces studied by sum frequency generation vibrational spectroscopy.Langmuir : the ACS journal of surfaces and colloids · 2012Review
- Interfacial orientation and secondary structure change in tachyplesin I: molecular dynamics and sum frequency generation spectroscopy studies.Langmuir : the ACS journal of surfaces and colloids · 2011Article
- Flagging fusion: Phosphatidylserine signaling in cell-cell fusion.The Journal of biological chemistryReview
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Select transmembrane proteins found in biogenic membranes are known to facilitate rapid bidirectional flip-flop of lipids between the membrane leaflets, while others have no little or no effect. The particular characteristics which determine the extent to which a protein will facilitate flip-flop are still unknown. To determine if the relative polarity of the transmembrane protein segment influences its capacity for facilitation of flip-flop, we have studied lipid flip-flop dynamics for bilayers containing the peptides WALP(23) and melittin. WALP(23) is used as a model hydrophobic peptide, while melittin consists of both hydrophobic and hydrophilic residues. Sum-frequency vibrational spectroscopy (SFVS) was used to characterize the bilayers and determine the kinetics of flip-flop for the lipid component, 1,2-distearoyl-sn-glycero-3-phosphocholine (DSPC), within the mixed bilayers. The kinetic data were utilized to determine the activation thermodynamics for DSPC flip-flop in the presence of the peptides. Melittin was found to significantly reduce the free energy barrier to DSPC flip-flop when incorporated into the bilayer at 1mol.%, while incorporation of WALP(23) at the same concentration led to a more modest reduction of the free energy barrier. The possible mechanisms by which these peptides facilitate flip-flop are analyzed and discussed in terms of the observed activation thermodynamics.
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