Tri-arginine insulins

Details Tri-arginine insulins Tri-arginine insulins

1993-07-06

1996-02-13

Warden, Jill

Chemistry: natural resins or derivatives; peptides or proteins;

Peptides of 3 to 100 amino acid residues

Insulin; related peptides

530324, A61K 3828, C07K 1462

Patent

active

054912164

ABSTRACT:
This invention relates to human insulin analogs (tri-arg insulins) and includes two enzymatic methods for producing tri-arg insulins. These compounds can be formulated as a soluble entity up to pH 6.1 and have prolonged hypoglycemic activity. Tri-arg insulins have the basic structure of natural human insulin plus three additional arginine residues. Two of the three additional Arg residues are located in tandem at the carboxy terminus of the insulin B-chain, and the third Arg residue is located at the amino terminus of the insulin A-chain. Tri-arg insulin analogs, having certain amino acid substitutions at the B3, B10 and A21 positions, are within the instant invention.

REFERENCES:
patent: 4569791 (1986-02-01), Frank et al.
patent: 4569792 (1986-02-01), Frank et al.
patent: 4581165 (1986-04-01), Frank et al.
patent: 4608364 (1986-04-01), Grau
patent: 4701440 (1987-10-01), Grau
patent: 4992418 (1991-02-01), Katsoyannis et al.
patent: 5008241 (1991-04-01), Markussen et al.
patent: 5130236 (1992-07-01), Hoffmann
Receptor Binding and Biological Potency of Several Split Forms (Conversion Intermeidates) of Human Proinsulin, The Journal of Biological Chemistry, vol. 260, No. 26, Issue of Nov. 15, pp. 13989-13994, 1985.
Biochemical and Clinical Implications of Proinsilin Conversion Intermediates, B. D. Given, et al., J. Clin. Invest., vol. 76, 1398-1405, Oct. 1985.
Soluble, prolonged-acting insulin derivatives. I. Degree of protration and crystallizability of insulins substituted in the termini of the B-chain, J. Markussen, et al., Protein Engineering, vol. 1, No. 3, pp. 205-213, 1987.
Soluble, prolonged-acting insulin derivatives. II. Degree of protraction and crystallizability of insulins substituted in position A17, B8, B13, B27 and B30, J. Markussen, et al., Protein Engineering, vol. 1, No. 3, pp. 215-223, 1987.
Soluble, prolonged-acting insulin derivatives. III. Degree of protraction and crystallizability of insulins substituted in position A17, B8, B13, B27 and B30, J. Markussen, et al., Protein Engineering, vol. 2, No. 2, pp. 157-166, 1988.
In vitro activity of biosynthetic human diarginylinsulin, X. Zeuzem, et al., Diabetologia 33:65-71, 1990.
U.S. Ser. No. 07/447,486, Hoffmann, filed Dec. 7, 1989.

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