Process for the synthesis of a peptide having a Trp residue

Details Process for the synthesis of a peptide having a Trp residue Process for the synthesis of a peptide having a Trp residue

2006-10-17

2006-10-17

Tsang, Cecilia J. (Department: 1654)

Chemistry: natural resins or derivatives; peptides or proteins;

Peptides of 3 to 100 amino acid residues

Synthesis of peptides

C530S334000, C530S335000, C530S337000, C530S344000, C530S345000, C530S328000

Reexamination Certificate

active

07122628

ABSTRACT:
A process for the solid phase synthesis of a peptide having at least one thyptophan residue, wherein said method comprises temporarily protecting the indole ring of said tryptophan residue with a side chain protecting group which is labile to a base wherein said protecting group is removed during cleavage of said peptide from the solid support.

REFERENCES:
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Mery, J. et al., “Tryptophan Reduction and Histidine Racemization During Deprotection by Catalytic Transfer Hydrogenation and of an Analog of the Luteinizing Hormone Releasing Factor,” Int. J. of Peptide and Protein Res. 1988, 31 (4):412-419, XP008005285.
Pineda, J. L. et al., “Effect of GnRH Antagonist [ac-delta-3Pro-1, pFDPhe-2, DTrp-3, 6] GnRH, on Pulsatile Gonadotrop in Secretion in the Castrate Male Primate,” J. Clin. Endocrinology and Metabolism, 1983, 56(2):420-422, XP008005269.
Coy, D. H. et al., “Minimal side-chain protection can be a successful strategy in solid-phase peptide synthesis,” Int. J. Peptide Protein Res., 1979, 14:339-343.
Pipkorn, R. et al., “Histidine racemization in the synthesis of an analog of the lutenizing hormone releasing factor,” Int. J. Pep. Protein Res., 1986, 27:583-588.

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