ArticleThe journal of physical chemistry. B2012
Molecular interactions between cell penetrating peptide Pep-1 and model cell membranes.
Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Distinct adsorption behavior and structures of cell-penetrating peptides at a model lipid membrane interface: a heterodyne-detected vibrational sum frequency generation spectroscopy study.Chemical science · 2026Article
- Article
- Exploring the Chemical Features and Biomedical Relevance of Cell-Penetrating Peptides.International journal of molecular sciences · 2024Review
- Cancer-Targeting Applications of Cell-Penetrating Peptides.International journal of molecular sciences · 2024Review
- Size-Dependent Interactions of Lipid-Coated Gold Nanoparticles: Developing a Better Mechanistic Understanding Through Model Cell Membranes and in vivo Toxicity.International journal of nanomedicine · 2020Article
- Otoferlin C2F Domain-Induced Changes in Membrane Structure Observed by Sum Frequency Generation.Biophysical journal · 2019Article
- Nano-viscosimetry analysis of the membrane disrupting action of the bee venom peptide melittin.Scientific reports · 2019Article
- Counting charges on membrane-bound peptides.Chemical science · 2018Article
- Novel Rosaceae plant elicitor peptides as sustainable tools to control Xanthomonas arboricola pv. pruni in Prunus spp.Molecular plant pathology · 2018Article
- Diversity of plant defense elicitor peptides within the Rosaceae.BMC genetics · 2018Article
- Probing Site-Specific Structural Information of Peptides at Model Membrane Interface In Situ.Journal of the American Chemical Society · 2015Article
- Membrane interaction of antimicrobial peptides using E. coli lipid extract as model bacterial cell membranes and SFG spectroscopy.Chemistry and physics of lipids · 2015Article
- Unveiling the membrane-binding properties of N-terminal and C-terminal regions of G protein-coupled receptor kinase 5 by combined optical spectroscopies.Langmuir : the ACS journal of surfaces and colloids · 2014Article
- Site-specific orientation of an α-helical peptide ovispirin-1 from isotope-labeled SFG spectroscopy.The journal of physical chemistry. B · 2013Article
- Lipid Fluid-Gel Phase Transition Induced Alamethicin Orientational Change Probed by Sum Frequency Generation Vibrational Spectroscopy.The journal of physical chemistry. C, Nanomaterials and interfaces · 2013Article
- A common landscape for membrane-active peptides.Protein science : a publication of the Protein Society · 2013Review
- Membrane orientation of Gα(i)β(1)γ(2) and Gβ(1)γ(2) determined via combined vibrational spectroscopic studies.Journal of the American Chemical Society · 2013Article
- Dependence of Alamethicin Membrane Orientation on the Solution Concentration.The journal of physical chemistry. C, Nanomaterials and interfaces · 2013Article
- Elucidation of molecular structures at buried polymer interfaces and biological interfaces using sum frequency generation vibrational spectroscopy.Soft matter · 2013Article
- Article
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2 authors.
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Abstract
We investigated the molecular interactions of a cell penetrating peptide (CPP) Pep-1 with model cell membranes using sum frequency generation (SFG) vibrational spectroscopy, supplemented by attenuated total reflectance-Fourier transform infrared spectroscopy (ATR-FTIR). Hydrogenated and deuterated 1,2-dipalmitoyl-sn-glycero-3-phosphoglycerol (DPPG and dDPPG) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1'-rac-glycerol) (POPG) were used in the experiments to represent gel-phase and fluid-phase lipid bilayers, respectively. Our SFG results indicated that Pep-1 molecules adopted a β-sheet conformation when adsorbed to the surface of gel-phase DPPG lipid bilayers. When interacting with fluid-phase POPG lipid bilayers, Pep-1 adopted a mix of α-helical and β-sheet structures over a broad range of peptide concentrations. The orientation distribution of the α-helical Pep-1 segment associated with the fluid-phase bilayers was found to depend on the peptide concentration. SFG orientation analysis showed that Pep-1 molecules adopted an orientation nearly perpendicular to the plane of the bilayer for peptide concentrations of 0.28 and 1.4 μM. When the Pep-1 concentration was increased to 7.0 μM, combined SFG and ATR-FTIR measurements showed that Pep-1 molecules were associated with the bilayer with a broad orientation distribution. Our results demonstrated that lipid bilayer phase and peptide concentration affect the conformation and orientation of Pep-1 molecules associated with model cell membranes, which is crucial to the translocation process of CPPs. A combination of SFG and ATR-FTIR studies can be used to determine the conformation and orientation of CPPs interacting with model cell membranes in situ.
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