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© Valérie Choumet
Mosquitoes were orally infected with the chikungunya virus. Midguts were dissected at day 5 post-infection, fixed and permeabilised. Virus is shown in red (anti-E2 protein, cyanine 3), the actin network in green (phalloidin 548) and nuclei in blue (DAPI).
Publication : Biochemistry

Peptide secondary structure induced by a micellar phospholipidic interface: proton NMR conformational study of a lipopeptide

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Biochemistry - 10 Mar 1992

Macquaire F, Baleux F, Giaccobi E, Huynh-Dinh T, Neumann JM, Sanson A

Link to Pubmed [PMID] – 1547240

Biochemistry 1992 Mar;31(9):2576-82

The conformational change of the model peptide Ac-K-G-R-G-D-G-amide induced by a phospholipidic interface was investigated by proton nuclear magnetic resonance (1H NMR). In aqueous solution, the free peptide is highly flexible and disordered, even in the presence of deuterated dodecyl-phosphocholine (DPC-d38) micelles which mimic a membrane interface. The lipopeptide, obtained by grafting a lipid anchor [2,3-dipalmitoyl-D-(+)-glyceric acid] to the lysine side chain of the peptide, was studied by standard 2D 1H NMR spectroscopy combined with distance geometry and simulated annealing calculations. When anchored to a micelle interface, the peptide acquires a definite turn (II/I’) conformation. We were also able to describe precisely the conformation of the diacylglyceric fragment of the lipopeptide in a lipid environment and to establish the average orientation of the peptide segment with respect to the micelle surface.

http://www.ncbi.nlm.nih.gov/pubmed/1547240