HIV related peptides combination or fusion for use in HIV vaccine composition or as diagnostic means

A technology of action and immunogen, applied in the field of identifying and providing useful agents for the treatment and diagnosis, diagnostic and predictive reagents, capable of solving problems such as designing drugs and diagnostic/predictive methods

Inactive Publication Date: 2012-10-03
BIONOR IMMUNO
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0012] However, to date, the mechanisms of C5-associated immune activation are currently largely unknown, meaning that it has not been possible to rationally design drugs and diagnostic / predictive methods based on these mechanisms

Method used

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  • HIV related peptides combination or fusion for use in HIV vaccine composition or as diagnostic means
  • HIV related peptides combination or fusion for use in HIV vaccine composition or as diagnostic means
  • HIV related peptides combination or fusion for use in HIV vaccine composition or as diagnostic means

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0318] Combine or peptide using conventional methods for linear sequences

[0319] Preparation of APTKAKRRVVQREKR

[0320] The peptides were synthesized in amide form from the corresponding starting points according to the general description (hereinafter "Synthetic Overview") of F-moc synthesis (Atherton et al.

[0321] Purity (HPLC): greater than 90%.

[0322] Mass Spectrometry: Theoretical Molecular Weight: 1822.2

[0323] Experimental molecular weight: 1823.0ES+

[0324] Preparation of APTKAKR

[0325] The peptides were synthesized in amide form from the corresponding starting points according to the synthetic overview.

[0326] Purity (HPLC): greater than 90%.

[0327] Mass Spectrometry: Theoretical Molecular Weight: 769.6

[0328] Experimental molecular weight: 760.7ES+

[0329] Preparation of APTRAKR

[0330] The peptides were synthesized in amide form from the corresponding starting points according to the synthesis outline.

[0331] Purity (HPLC): greater tha...

Embodiment 2

[0444] Synthesis of complex peptides

[0445] Preparation of CGGAKRRVVGGAKRRVVGQREKRAV

[0446] |

[0447] CGGGDQQLLGGAEEEIVGGIEEEGGERDRD

[0448] Purity (HPLC): greater than 90%.

[0449] Theoretical molecular weight: 5750.4

[0450] Preparation of CGGAKRRVVGGAKRRVVGGQREKR

[0451] |

[0452] CGGGDQQLLGGAEEEIVGGIEEEGG

[0453] Purity (HPLC): greater than 90%.

[0454] Theoretical molecular weight: 4965.6

[0455] Preparation of CGGAEEEVVGGDQQLL

[0456] |

[0457] GCGGAKRRVVGGAKRRVV

[0458] Purity (HPLC): greater than 90%.

[0459] Theoretical molecular weight: 3410.9

[0460] Preparation:

[0461] GAKRRVVGG C GGAKRRVVQREKRAGEREKRA (SEQ ID NO: 38)

[0462] |

[0463] G K GGIEEEGGRDRDRGGEQDRDR (SEQ ID NO: 39)

[0464] Purity (HPLC): greater than 94%.

[0465]Theoretical molecular weight: 5876.93

Embodiment 3

[0467] Recognition of SEQ ID NO: 1 alone and in combination with SEQ ID NO: 6, 8 and 9 by pooled human sera from HIV chronically infected individuals, LTNP and non-infected blood donors

[0468] Sera of SEQ ID NO: 1 alone or in combination with SEQ ID NO: 6 (having the sequence DRPEGIEEEEGGERDR), 8 and 9 were determined according to general ELISA principles using magnetic particles as solid support or immobilization of peptides to 96-well plates Reactivity (seroreactivity).

[0469] method:

[0470] In the system described below, peptides are coated on magnetic particles using recognized techniques. For all peptides, 300 μg was coated on the particles except for SEQ ID NO: 1 where 600 μg was used. SEQ ID NO: 1 (from C5) and SEQ ID NO: 6, 8 and 9 (from gp41) were pre-incubated overnight at 4°C to allow interactions between the C5 and gp41 sequences, respectively, and all combinatorially. Sera were then incubated with peptide-coated beads according to established protocols. ...

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PUM

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Abstract

Disclosed is a method for treatment of HIV related diseases comprising targeting complexes between on the one hand the C5 domain of gpl20 and on the other hand gp41 or the C2 domain of gpl20. The complexes may be stabilised by administering compounds, such as antibodies, capable of directly interacting with and stabilising the complex, or by immunizing with C5 and gp41/C2 derived material so as to induce antibodies that bind to and stabilise the complex.

Description

field of invention [0001] The present invention relates to novel agents and methods for the treatment, diagnosis and prognosis of HIV infection and AIDS, and the present invention further relates to methods for identifying and providing agents useful for said treatment and diagnosis. [0002] In particular, the present invention relates to novel therapeutic agents capable of affecting the stability of complexes between domains in specific HIV proteins, and to diagnostic and prognostic reagents useful for indicating the presence of such agents. Background of the invention [0003] In recent years, a large body of research evidence has accumulated that supports the concept that AIDS is an immune disease caused by HIV-1 and not simply caused by the loss of CD4+ T lymphocytes as a result of chronic cytopathic viral infection. It is therefore important to develop interventions that also target the chronic immune stimulation caused by HIV-1. [0004] Previous studies have shown t...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): A61K38/16A61K39/21A61K39/00A61K39/395A61K39/42C07K16/10C07K19/00
CPCC12N2740/16134C07K16/1063C12N2740/16122A61K39/21A61K2039/53A61K2039/5258C07K14/005A61K2039/505A61K39/12A61K2039/545A61P31/18A61K2039/627C12N7/00C12N2740/16171
Inventor 马亚·索默费尔特·格伦沃尔安格斯·达格利什埃纳·滕内斯·兰格延斯·奥勒夫·霍姆伯格佩尔·本特松比格尔·索伦森
Owner BIONOR IMMUNO
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