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Influence of silaproline on peptide conformation and bioactivity
Florine Cavelier1, Bertrand Vivet, Jean Martinez
1Laboratoire des Amino acides, Peptides et Protéines, UMR-CNRS 5810, Universités de Montpellier I et II, UM II, CC19-34095 Montpellier Cedex 05, France.
Abstract:
The analogue gamma-(dimethylsila)-proline, denoted silaproline (Sip), was synthesized in both enantiomerically pure forms by diastereoselective alkylation of a chiral glycine equivalent with use of Schöllkopf's bis-lactim ether method. The effect of replacing a proline residue in model peptides by this new proline surrogate has been examined in the crystal state by X-ray diffraction and in solution by IR absorption and NMR techniques. Silaproline and proline-containing sequences exhibit very similar conformational properties. Silaproline was also substituted for proline in a neurotensin (8-13) analogue that retained biological activity and exhibited enhanced resistance to biodegradation.
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