ArticleBiophysical journal2000
Detection of peptide-lipid interactions in mixed monolayers, using isotherms, atomic force microscopy, and fourier transform infrared analyses.
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Biomimetic Models to Investigate Membrane Biophysics Affecting Lipid-Protein Interaction.Frontiers in bioengineering and biotechnology · 2020Review
- Effect of clay nanoparticles on model lung surfactant: a potential marker of hazard from nanoaerosol inhalation.Environmental science and pollution research international · 2016Article
- Roles of hydrophobicity and charge distribution of cationic antimicrobial peptides in peptide-membrane interactions.The Journal of biological chemistry · 2012Article
- Bioactivities of simplified adociaquinone B and naphthoquinone derivatives against Cdc25B, MKP-1, and MKP-3 phosphatases.Bioorganic & medicinal chemistry · 2009Article
- Investigations into the ability of the peptide, HAL18, to interact with bacterial membranes.European biophysics journal : EBJ · 2008Article
- Coexistence of a two-states organization for a cell-penetrating peptide in lipid bilayer.Biophysical journal · 2005Article
- Viral membrane penetration: lytic activity of a nodaviral fusion peptide.European biophysics journal : EBJ · 2005Article
- Interactions of the human calcitonin fragment 9-32 with phospholipids: a monolayer study.Biophysical journal · 2004Article
- Aggregation of puroindoline in phospholipid monolayers spread at the air-liquid interface.Biophysical journal · 2003Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To improve the understanding of the membrane uptake of an amphipathic and positively charged vector peptide, we studied the interactions of this peptide with different phospholipids, the nature of whose polar headgroups and physical states were varied. Three lipids were considered: dipalmitoylphosphatidylcholine (DPPC), dipalmitoylphosphatidylglycerol (DPPG), and dioleoylphosphatidylglycerol (DOPG). The approach was carried out by three complementary methods: compression isotherms of monolayers and atomic force microscopy observations associated with Fourier transform infrared investigations. From analysis of the compression isotherms, it was concluded that the peptide interacts with all lipids and with an expansion of the mean molecular area, implying that both components form nonideal mixtures. The expansion was larger in the case of DOPG than for DPPC and DPPG because of an alpha to beta conformational transition with an increase in the peptide molar fraction. Atomic force microscopy observations showed that the presence of small amounts of peptide led to the appearance of bowl-like particles and that an increase in the peptide amounts generated the formation of filaments. In the case of DOPG, filaments were found at higher peptide molar fractions than already observed for DOPC because of the presence of negatively charged lipid headgroups.
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Registered trials
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