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Site 2 insulin analogues

A technology of insulin analogs and insulin, applied in the direction of insulin, hormone peptides, drug combinations, etc., can solve problems such as disturbing modification or substitution

Inactive Publication Date: 2016-01-06
CASE WESTERN RESERVE UNIV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Therefore, it is expected that modifications or substitutions that generally introduce modest perturbations of IR binding in the insulin molecule will be well tolerated in vivo as assessed in vitro, and in terms of potency or (in the absence of an effect on self-assembly) Indistinguishable from wild-type insulin in terms of other pharmacological properties—or even more potent and as in 2-F-Phe B24 -In case of DKP-insulin prolonged

Method used

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  • Site 2 insulin analogues
  • Site 2 insulin analogues
  • Site 2 insulin analogues

Examples

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Embodiment Construction

[0026] The present invention relates to double-chain or single-chain insulin analogues which provide (i) rapid absorption from subcutaneous depots, and (ii) shortened duration of action with similar ratios of IR-A / IR-B receptor binding affinities that of wild-type insulin with an absolute affinity in the range of 5-100% (the lower limit was chosen to correspond to proinsulin). Examples of B-chain substitutions that confer rapid absorption are aspartic acid or lysine at position B28, optionally in combination with proline at position B29. Removal of the proline from position B28 was associated with reduced intensity of dimerization and hexamer assembly independent of the nature of the substituted amino acid. Yet another example of a B-chain substitution that confers rapid absorption is the combination of lysine at position B3 and glutamic acid at position B29 when formulated in the absence of zinc ions. Amino acid substitutions introduced to achieve reduced signaling duration ...

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Abstract

An insulin analogue contains one or more modifications at a distinct protein surface comprising one or more of the residues at position B13, B17, A12, A13, and / or A17. Formulations of the above analogues at successive strengths U-100 to U-1000 in soluble solutions a at least pH value in the range 6.8-8.0 either in the presence of zinc ions at a molar ratio of 2.2-10 zinc ions per six insulin analogue monomers or in the presence of fewer than 1 zinc ions per six insulin analogue monomers. Use of the above formulation in an insulin pump functionally integrated with a continuous glucose monitor and computer-based control algorithm as a closed-loop system. A method of treating a patient with diabetes mellitus comprises administering a physiologically effective amount of the insulin analogue to a patient by means of intravenous, intraperitoneal, or subcutaneous injection.

Description

[0001] Statement Regarding Federally Funded Research or Development [0002] This invention was made with Government support under a collaborative agreement awarded by the National Institutes of Health under grant numbers DK040949 and DK074176. The US Government may have certain rights in this invention. Background of the invention [0003] The present invention relates to polypeptide hormone analogs which exhibit enhanced pharmaceutical properties, such as altered pharmacokinetic and pharmacodynamic properties, i.e. conferring a shortened duration of action relative to soluble formulations of the corresponding wild-type human hormone . More particularly, the present invention relates to insulin analogs containing (i) one or more of Amino acid substitutions, the one or more B chain substitutions are known in the art to accelerate the absorption of insulin analogues from subcutaneous depots into the bloodstream. The insulin analogs of the invention may optionally contain a l...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): A61K38/28C07K14/62C07H21/04
CPCA61K38/00C07K14/62A61P3/10
Inventor M.A.维斯
Owner CASE WESTERN RESERVE UNIV
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