International Journal of Peptide and Protein Reseach 1994-04-01

Synthesis of disulfide-bridged fragments of omega-conotoxins GVIA and MVIIA. Use of Npys as a protecting/activating group for cysteine in Fmoc syntheses.

R G Simmonds, D E Tupper, J R Harris

Index: Int. J. Pept. Protein Res. 43(4) , 363-6, (1994)

Full Text: HTML

Abstract

The 3-nitro-2-pyridinesulphenyl (Npys) moiety is finding increasing utility as a protecting-activating group for cysteine, particularly in the synthesis of cyclic and unsymmetrical disulfides using the Boc strategy. This chemistry has been extended to peptides assembled by the Fmoc strategy. N-Terminal Cys(Npys) is introduced via Boc-Cys(Npys)-OPfp. Non-N-terminal Cys(Npys) is incorporated by reacting a resin-bound, fully protected Cys(Acm) peptide with NpysCl. This approach has been applied to the synthesis of four disulfide-bridged fragments of omega-conotoxins GVIA and MVIIA.


Related Compounds

Related Articles:

Synthesis and stability of 3-nitro-2-pyridinesulfenyl chloride (NpysCl).

1993-11-01

[Int. J. Pept. Protein Res. 42(2) , 159-64, (1993)]

Discriminative affinity labelling of opioid receptors by enkephalin and morphiceptin analogues containing 3-nitro-2-pyridinesulphenyl-activated thiol residues.

[J. Chromatogr. A. 597(1-2) , 425-8, (1992)]

Compatibility of the S-(3-nitro-2-pyridinesulfenyl) protecting group with DCC/HOBt coupling chemistry.

1992-01-01

[Pept. Res. 5(5) , 262-4, (1992)]

Thiolysis of the 3-nitro-2-pyridinesulfenyl (Npys) protecting group. An approach towards a general deprotection scheme in peptide synthesis.

1990-06-01

[Int. J. Pept. Protein Res. 35(6) , 545-9, (1990)]

Design and synthesis of a kininogen-based selective inhibitor of thrombin-induced platelet aggregation.

1994-01-01

[Pept. Res. 7 , 32-35, (1994)]

More Articles...