Segregated folding determinants for small disulfide-rich peptide

Details Segregated folding determinants for small disulfide-rich peptide Segregated folding determinants for small disulfide-rich peptide

1991-04-18

1993-07-27

Wax, Robert A.

Chemistry: molecular biology and microbiology

Micro-organism, tissue cell culture or enzyme using process...

Recombinant dna technique included in method of making a...

435 681, 435 691, 4351723, 530333, 530300, 530334, 530338, 530857, 530350, C12P 2106, C12P 2100, C07K 700, C07K 1500

Patent

active

052310116

ABSTRACT:
The preparation of small peptides with multiple disulfide bonds is accomplished by forming a prepropeptide with an N-terminal excised region separated from the cysteine-rich peptide by one or more cleavable amino acid residues. The excised region preferably consists of an N-terminal end providing a hydrophobic signal sequence domain having up to approximately 25 amino acids, and an intermediate central propeptide domain having a variable length of between about 5-50 amino acids. The N-terminal excised region serves as a folding template to direct the formation of specific disulfide bonds in the cysteine-rich peptide. The cysteine-rich peptide is cleaved by enzymes releasing the biologically active peptide.

REFERENCES:
Olivera et al. (1990) Science, vol. 249, Jul. 1990, pp. 257-263.
Olivera et al. (1987), Biochemistry, vol. 26, No. 8, 1987, pp. 2086-2090.
Woodward et al., Eubo Journal, vol. 9, No. 4, pp. 1015-1020, 1990.
Becker et al., Eur. J. Biochem, vol. 185, 1989, pp. 79-84.
Hillyard et al., Biochemistry, vol. 28, No. 1, 1989, pp. 358-361.
Cruz et al., Biochemistry, vol. 28, No. 8, 1989, pp. 3437-3442.

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