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Proteinaceous pharmaceuticals and uses thereof

A protein and cysteine ​​technology, which is applied to peptide/protein components, pharmaceutical formulations, medical preparations containing active ingredients, etc., can solve the problems of no definite folding, no single stable structure, etc.

Inactive Publication Date: 2009-11-18
阿穆尼克斯公司
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Different types of libraries are random peptide or cyclic peptide libraries, but these are not considered proteins as they do not have any defined fold and do not adopt a single stable structure

Method used

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  • Proteinaceous pharmaceuticals and uses thereof
  • Proteinaceous pharmaceuticals and uses thereof
  • Proteinaceous pharmaceuticals and uses thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0912] Example 1: Randomization of CDP 6_6_12_3_2

[0913] The following examples describe the design of CDP 6_6_12_3_2 based libraries. Partial sequences matching CDP 6_6_12_3_2 were searched in the TrEMBL protein sequence database. A total of 71 sequences matched this CDP. Calculate the amino acid abundance for each site as shown in Table 5. For each non-cysteine ​​site, we selected a randomization scheme based on the following criteria: a) avoiding the introduction of stop codons, b) avoiding the introduction of additional cysteine ​​residues, c) allowing for >3% specific position where a large number of amino acids were observed, d) minimized the incorporation of amino acids not observed in any of the 71 native sequences matching this CDP.

[0914]

[0915]

Embodiment 2

[0916] Example 2: Protein expression and folding in E. coli

[0917] The oligonucleotides were cloned into expression plasmid vectors driving protein expression in E. coli cytoplasm. A preferred promoter is T7 (Novagen pET vector series; Kan marker) in E. coli strain BL21 DE3. A preferred method of inserting these oligos is the modified Kunkel method (Scholle, D., Kehoe, JW and Kay, B.K. (2005) Efficient construction of a large collection of phage-displayed combinatorial peptide libary. Comb. Chem. & HTP Screening8: 545-551). A different approach is to perform 2-oligo PCR on (full or partial) vectors, followed by digestion of unique restriction sites in the ends of the oligo-derived fragments, followed by ligation of matching non-palindromic overhangs (effective fragment inner join). The third method is to assemble the insert from 2 or 4 oligos by overlapping PCR, digest restriction sites at the end of the assembled insert, and then ligate it into the digested vector. Tran...

Embodiment 3

[0919] Embodiment 3: Design steps of antifreeze protein

[0920] Purpose: Design libraries for antifreeze repeat proteins

[0921] Strategy: The starting sequence for library design was derived from antifreeze protein from Tenebrio molitor (Genbank accession number AF160494). This protein is known to express well in E. coli. Both crystal and NMR structures can be obtained. The protein is built from repeating units that form cylinders. The core of the structure lacks hydrophobic amino acids, but each repeat unit contains a disulfide bond and an invariant serine and alanine residue. The first two figures form a capping motif with three disulfide bonds. This capping motif is speculated to form a folded core. Thus, the first two repeat units generally remain unchanged during in vitro evolution. see Figure 127 .

[0922] Structural features of antifreeze proteins were analyzed in order to select exchange points and to discover glutamine residue sites for Scholle mutagenesi...

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Abstract

The present invention provides cysteine-containing scaffolds and / or proteins, expression vectors, host cell and display systems harboring and / or expressing such cysteine-containing products. The present invention also provides methods of designing libraries of such products, methods of screening such libraries to yield entities exhibiting binding specificities towards a taraget molecule. Further provided by the invention are pharmaceutical compositions comprising the cysteine-containing products of the present invention.

Description

[0001] cross reference [0002] This application claims priority to U.S. Provisional Application Nos. 60 / 721,270 and 60 / 721,188, filed September 27, 2005, and U.S. Provisional Application No. 60 / 743,622, filed March 21, 2006, which It is incorporated herein by reference. Background of the invention [0003] A fundamental concept of molecular biology is that each native protein adopts a single "native" structure or fold. The adoption of any fold other than the native fold is considered a "misfold". There are few or no examples of native proteins employing multiple native functional folds. Misfolding is a serious problem, as is the infectivity of prions, whose "misfolding" causes other prion proteins to misfold catalytically, and leads to encephalopathy and some death. Almost any protein can misfold when denatured, forming fibrous polymers that appear to be involved in many degenerative diseases. An example is the beta-amyloid fibrils associated with Alzheimer's disease. M...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): A61K38/00C07K1/00
Inventor W·P·C·斯泰默V·舍伦贝格尔M·巴德尔M·肖勒
Owner 阿穆尼克斯公司
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