Slightly modifying pseudoproline dipeptides incorporation strategy enables solid phase synthesis of a 54 AA fragment of caveolin-1 encompassing the intramembrane domain.
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.
Coïc
Yves-Marie
YM
Unité de Chimie des Biomolécules, URA CNRS 2128, Institut Pasteur, 28 rue du Docteur Roux, F-75724, Paris Cedex 15, France. yves-marie.coic@pasteur.fr
Lan
Charlotte Le
CL
Neumann
Jean-Michel
JM
Jamin
Nadège
N
Baleux
Françoise
F
D000595:Amino Acid Sequence; D051242:Caveolin 1 / Q000138:chemical synthesis* / Q000737:chemistry; D002851:Chromatography, High Pressure Liquid; D004151:Dipeptides / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008565:Membrane Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D011392:Proline / Q000031:analogs & derivatives* / Q000737:chemistry; D013844:Thiazoles / Q000737:chemistry*
D051242:Caveolin 1; D004151:Dipeptides; D008565:Membrane Proteins; D013844:Thiazoles; C505976:pseudoproline; D011392:Proline