ArticleEuropean biophysics journal : EBJ2003
Effect of cholesterol on bilayer location of the class A peptide Ac-18A-NH2 as revealed by fluorescence resonance energy transfer.
Article in European biophysics journal : EBJ, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 12 citations in OpenAlex.
- Fӧrster resonance energy transfer analysis of amyloid state of proteins.BBA advances · 2022Article
- Lipid Bilayer Interactions of Amyloidogenic N-Terminal Fragment of Apolipoprotein A-I Probed by Förster Resonance Energy Transfer and Molecular Dynamics Simulations.Journal of fluorescence · 2018Article
- Apolipoprotein A-I mimetic peptide 4F blocks sphingomyelinase-induced LDL aggregation.Journal of lipid research · 2015Article
- Interaction of melittin with membrane cholesterol: a fluorescence approach.Biophysical journal · 2004Article
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An amphipathic class A peptide, Ac-18A-NH(2), has been employed in modeling the alpha-helical lipid-binding site of apolipoprotein A-I (apoA-I). To gain insight into the nature of protein-lipid interactions responsible for the ability of apoA-I to promote the efflux of intracellular cholesterol, the peptide disposition in model membranes composed of phosphatidylcholine (PC) and its mixture with cholesterol (Chol) has been characterized. By examining resonance energy transfer between the peptide Trp as a donor and anthrylvinyl-labeled PC as an acceptor it was found that Chol inclusion is conducive to shallower bilayer location of the Ac-18A-NH(2) alpha-helix. The limits for the Trp distance from the membrane center were estimated to be 1.5-1.7 nm (PC) and 1.9-2.1 nm (PC:Chol), indicating that in the PC bilayer the Trp resides at the level of the glycerol backbone and carbonyl groups while the region of the phosphocholine moieties is preferable for Trp location in the PC:Chol bilayer. These findings suggest that Chol can modulate the interactions between apoA-I and membrane lipids via reducing the depth of alpha-helix bilayer penetration.
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