Compounds, compositions and uses thereof for improvement of bone disorders

a technology of compounds and compounds, applied in the field of compounds, can solve the problems of long peptides being dangerous for patients, long peptides are usually rapidly degraded, and the manufacturing process is extensive and expensive, so as to prevent or treat bone disorders

Inactive Publication Date: 2019-11-21
AMOLYT PHARMA
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Longer peptides are usually rapidly degraded following administration and their in vivo efficacy is often weak following intravenous, subcutaneous or intramuscular bolus administration.
In addition, manufacturing long peptide is an extensive and expensive process, whether it is manufactured by solid-phase peptide synthesis or by recombinant technology.
Finally, chronically treating patients with a long peptide might represent safety risks for the patients in the form of immunogenicity.
Raising neutralizing antibodies against a natural peptide is a potential major health risk for the patients.

Method used

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  • Compounds, compositions and uses thereof for improvement of bone disorders
  • Compounds, compositions and uses thereof for improvement of bone disorders
  • Compounds, compositions and uses thereof for improvement of bone disorders

Examples

Experimental program
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Effect test

example 1

HBD1 Fragments on Osteocalcin Expression During In Vitro Osteoblast Differentiation

[0124]Peptides were manufactured according to a standard manufacturing process in peptide chemistry by solid phase peptide synthesis (SPPS) using the Fmoc (9-fluorenylmethyloxycarbonyl) strategy (Merrifield, R. B. Solid phase peptide synthesis. I. The synthesis of a tetrapeptide. J. Am. Chem. Soc. 1963, 85, 2149-2154). Identity of the peptides was verified by LC-MS. The purity (at least 95%) and the net peptide content of peptides were determined by RP-HPLC and elemental analysis, respectively.

[0125]Each peptide was tested in a biologic assay measuring its ability to stimulate differentiation of osteoblast cells over a 18-21 day interval (Table 8) or a 14-15 day interval (Table 9) as assessed by the stimulation of osteocalcin protein synthesis. MC-3T3 E1 clone 4 (CL4) osteoblast cells were obtained from ATCC (Manassas, Va., USA). Cells were cultured in α-MEM containing 10% fetal bovine serum (FBS; The...

example 2

f Various Doses of HBD1 Fragments on Osteocalcin Expression During In Vitro Osteoblast Differentiation

[0127]The HBD1 (3-11) peptide as set forth in SEQ ID NO: 10 was manufactured according to a standard manufacturing process in peptide chemistry by solid phase peptide synthesis (SPPS) using the Fmoc (9-fluorenylmethyloxycarbonyl) strategy (Merrifield, R. B. Solid phase peptide synthesis. I. The synthesis of a tetrapeptide. J. Am. Chem. Soc. 1963, 85, 2149-2154). The identity of the peptide was verified by LC-MS. The purity (at least 95%) and the net peptide were determined by RP-HPLC and elemental analysis, respectively.

[0128]The peptide was tested at different concentrations in a biologic assay measuring its ability to stimulate differentiation of osteoblast cells over a 18 day interval as assessed by the stimulation of osteocalcin protein synthesis. MC-3T3 E1 clone 4 (CL4) osteoblast cells were obtained from ATCC (Manassas, Va., USA). Cells were cultured in α-MEM containing 10% fe...

example 3

HBD1 Fragment Analogs with Alanine Substitutions on Osteocalcin Expression During In Vitro Osteoblast Differentiation

[0130]The peptides were manufactured according to a standard manufacturing process in peptide chemistry by solid phase peptide synthesis (SPPS) using the Fmoc (9-fluorenylmethyloxycarbonyl) strategy (Merrifield, R. B. Solid phase peptide synthesis. I. The synthesis of a tetrapeptide. J. Am. Chem. Soc. 1963, 85, 2149-2154). Identity of peptides was verified by LC-MS. The purity (at least 95%) and the net peptide content of peptides were determined by RP-HPLC and elemental analysis, respectively.

[0131]Each peptide was tested in a biologic assay measuring its ability to stimulate differentiation of osteoblast cells over a 15 day interval as assessed by the stimulation of osteocalcin protein synthesis. MC-3T3 E1 clone 4 (CL4) osteoblast cells were obtained from ATCC (Manassas, Va., USA). Cells were cultured in α-MEM containing 10% fetal bovine serum (FBS; Thermo Fisher Sc...

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Abstract

The present technology generally relates to peptides of IGFBP-2 that may be used to improve bone disorders. The present technology also generally relates to uses of such peptides in methods for preventing or treating bone disorders and to compositions for such uses.

Description

CROSS-REFERENCE TO RELATED APPLICATION[0001]The present application claims priority to and benefit from U.S. Provisional Patent Application 62 / 455,124, filed on Feb. 6, 2017, the disclosure of which is incorporated herein by reference in its entirety.FIELD OF TECHNOLOGY[0002]The present technology generally relates to compounds, in particular peptides that may be used to improve bone disorders. The present technology also generally relates to uses of such compounds in methods for preventing and / or treating bone disorders and to compositions for such uses.BACKGROUND INFORMATION[0003]Insulin-like growth factor binding protein-2 (IGFBP-2) is a 36,000 Dalton protein that is a member of the IGFBP family. There are six (6) forms of high affinity IGF binding proteins. In addition to binding the insulin-like growth factors I and II and acting as transport proteins, these proteins have been shown to have some actions that are independent of their ability to bind to IGFs.[0004]IGFBP-2 is the ...

Claims

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Application Information

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Patent Type & Authority Applications(United States)
IPC IPC(8): C07K14/47A61P19/10
CPCC07K14/4743A61P19/10A61K38/00C07K7/06A61K38/08A61K38/1754A61P19/08
Inventor CLEMMONS, DAVIDXI, GANGDELALE, THOMASJULIEN, MICHELABRIBAT, THIERRY
Owner AMOLYT PHARMA
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