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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 : Journal of peptide science : an official publication of the European Peptide Society

Slightly modifying pseudoproline dipeptides incorporation strategy enables solid phase synthesis of a 54 AA fragment of caveolin-1 encompassing the intramembrane domain

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of peptide science : an official publication of the European Peptide Society - 01 Feb 2010

Coïc YM, Lan CL, Neumann JM, Jamin N, Baleux F

Link to Pubmed [PMID] – 20014324

J. Pept. Sci. 2010 Feb;16(2):98-104

This work contributes to highlight the benefits of pseudoproline dipeptides introduction in difficult SPPS. We show how a slight modification in the positioning choice conditioned the synthesis achievement of a 54 amino acid long caveolin-1 peptide encompassing the intramembrane domain. Furthermore, we report a side reaction correlated with the coupling steps and generating truncated fragments with a mass deviation of + 42 Da. Considering the need of structural data for membrane proteins, most of which are considered as prevalent therapeutic targets, chemical synthesis provides an interesting alternative pathway to obtain hydrophobic domains by pushing back the frontiers of conventional RP methods of purification.

http://www.ncbi.nlm.nih.gov/pubmed/20014324