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Form board stationary beta hair clip ring analog and use in bacteriophage exhibition

A technology of immobilizing templates and mimetics, which is applied in the direction of microbial libraries, peptide preparation methods, chemical libraries, etc., can solve problems such as separation of affinity ligands, and achieve the effect of promoting strong activity and promoting binding-activity research

Inactive Publication Date: 2010-03-24
POLYPHOR AG +1
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0007] These loops exhibit a limited number of conformations, which may lead to segregation of the affinity ligand for the receptor target

Method used

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  • Form board stationary beta hair clip ring analog and use in bacteriophage exhibition
  • Form board stationary beta hair clip ring analog and use in bacteriophage exhibition
  • Form board stationary beta hair clip ring analog and use in bacteriophage exhibition

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0247] Example 1 (n=8) is shown in Table 1. Starting with the amino acid Cys, the peptide was synthesized, and the Cys was grafted onto the resin. The starting resin was Fmoc-Cys(Trt)-chlorotrityl resin (prepared as described above). Linear peptides were synthesized on solid supports according to Procedure 1 in the following order: Resin-Cys-P8-P7-P6-P5-P4-P3-P2-P1-Cys, followed by acylation, cleavage, deprotection as indicated , purification and cyclization. HPLC retention time (min) and mass determined using the above gradient: RT = 7.26 min, [M+H] + = 1281.3.

Embodiment 2

[0248] Example 2 (n=8) is shown in Table 1. Starting with the amino acid Lys, the peptide was synthesized, and Lys was grafted onto the resin. The starting resin was Fmoc-Lys(Boc)-chlorotrityl resin (prepared as above). Synthesize linear peptides on a solid support according to Procedure 1 in the following order: Resin-R2 -Cys-P8-P7-P6-P5-P4-P3-P2-P1-Cys-R 1 , followed by acylation, cleavage, deprotection, purification and cyclization of the peptide as indicated. HPLC retention time (min) and mass determined using the above gradient: RT = 6.41 min, [M+H] + = 871.4.

Embodiment 3

[0249] Example 3 (n=10) is shown in Table 2. Starting with the amino acid Cys, the peptide was synthesized, and the Cys was grafted onto the resin. The starting resin was Fmoc-Cys(Trt)-chlorotrityl resin (prepared as above). Synthesize linear peptides on a solid support according to Procedure 1 in the following order: Resin-Cys-P10-P9-P8-P7-P6-P5-P4-P3-P2-P1-Cys, and then acylate the peptides as indicated. Synthesis, fragmentation, deprotection, purification and cyclization. HPLC retention time (min) and mass determined using the above gradient: RT = 5.74 min, [M+H] + = 779.2.

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Abstract

Template-fixed beta-hairpin mimetics of the general formula R<1>-Cys-Z-Cys-R<2> (I) wherein the two Cys residues are bridged by a disulfide bond thereby forming a cyclic peptide; R<l> and R<2> are preferably Glu-Thr and Thr-Lys; or Lys-Thr and Thr-Glu; or Thr-Glu and Lys-Thr; or Thr-Lys and Glu-Thr; or Leu-Glu and Lys-Val; or Val-Lys and Glu-Leu; or Glu-Leu and Val-Lys; or Lys-Leu and Val-Glu; orAsn-Gly and Lys-Val; or Val-Gly and Lys-Asn; or Gly-Asn and Val-Lys; or Gly-Val and Asn-Lys; or Gly-Gly and Gly-Gly; or Glu-Leu-Lys and Glu-Val-Lys; or Lys-Val-Glu and Lys-Leu-Glu; or Leu-Glu-Lys andGlu-Lys-Val; or Val-Lys-Glu and Lys-Glu-Leu; or Glu-Lys-Leu and Val-Glu-Lys; or Lys-Glu-Val and Leu-Lys-Glu; or Lys-Glu-Leu and Val-Lys-Glu; or Glu-Lys-Val and Leu-Glu-Lys; or Lys-Val-Gly and Gly-Leu-Glu; or Glu-Leu-Gly and Gly-Val-Lys; or Val-Lys-Gly and Gly-Glu-Leu; or Leu-Glu-Gly and Gly-Lys-Val; or Val-Gly-Lys and Glu-Gly-Leu; or Leu-Gly-Glu and Lys-Gly-Val; or Gly-Gly-Gly and Gly-Gly-Gly; andZ is a chain of n amino acid residues with n being an integer form 4 to 20 and with each of these n amino acid residues being, independently, derived from any naturally occurring L- alpha-amino acidare provided.

Description

technical field [0001] The present invention relates to compositions and methods of certain peptide sequences consisting of naturally occurring L-alpha-amino acid residues, wherein certain amino acid residues are bridged by disulfide bonds according to their position in the chain cysteine, thereby forming a cyclic peptide; and, certain other amino acid residues adjacent to said cysteine ​​form a certain type of di- or tripeptide moiety as defined below, which together serve as a template to Conducive to the formation and stability of the β-hairpin loop structure. Given the stability and confinement of these template-immobilized hairpin loop mimics, they may exhibit higher or prolonged activity against protein-binding partners. [0002] Templates can be embedded in the construction of hairpin loop mimics from phage display for library screening and drug screening. The compositions and methods of the invention can be used to screen and identify interacting proteins in vitro. ...

Claims

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Application Information

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Patent Type & Authority Patents(China)
IPC IPC(8): C12N15/10C07K7/04C07K1/04C40B40/02
CPCC40B40/02C07K1/047C12N15/1037
Inventor J·W·维瑞吉布罗德D·奥布瑞彻特S·罗库里欧F·O·格姆勃特C·卢丁F·荣格
Owner POLYPHOR AG
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