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US 10,703,792 B2Granted
Insulin analogues with selective signaling properties and reduced mitogenicity
AssigneeCase Western Reserve University
InventorMichael A. Weiss
Life of this patent
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AssigneeCase Western Reserve University
InventorMichael A. Weiss
Estimating the term…
A two-chain insulin analogue contains Aspartic Acid at position B10 and penta-fluoro-Phenylalanine at position B24, optionally Histidine or Glutamic Acid at position A8, optionally additional substitutions or modifications at positions A13 and/or A14 and/or B28 and/or B29. The analogue may be an analogue of a mammalian insulin, such as human insulin, may optionally include (i) N-terminal deletion of one, two or three residues from the B chain, (ii) a mono-peptide or dipeptide C-terminal extension of the B-chain containing at least one acidic residue, and (iii) other modifications known in the art to enhance the stability of insulin. Formulations of the above analogues at successive strengths U-100 to U-1000 in soluble solutions at at least pH value in the range 7.0-8.0 in the absence or presence of zinc ions at a molar ratio of 0.00-0.10 zinc ions per insulin analogue monomer.
An insulin analogue comprising a B-chain polypeptide containing an Asp substitution at position B10 relative to wild type human insulin and a penta-fluoro-Phe substitution at position B24 relative to wild type human insulin, and additionally comprising a Glu substitution at position B29 relative to wild type human insulin.
An insulin analogue comprising a B-chain polypeptide containing an Asp substitution at position B10 relative to wild type human insulin and a penta-fluoro-Phe substitution at position B24 relative to wild type guman insulin, and additionally comprising an N-terminal deletion of the B-chain polypeptide of one to three amino acids.
An insulin analogue comprising a B-chain polypeptide containing an Asp substitution at position B10 relative to wild type human insulin and a penta-fluoro-Phe substitution at position B24 relative to wild type human insulin, and additionally comprising an A-chain polypeptide containing one or more of the substitutions, relative to wild type human insulin, selected from the group consisting of:
Dependencies are inferred from the claim text.