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Synthetic immunoglobulin domains with binding properties engineered in regions of the molecule different from the complementarity determining regions

a technology of immunoglobulin and binding properties, applied in the field of libraries of immunoglobulins, can solve the problems of peptide grafting into a non-cdr loop, difficult to further modify the structural loop without changing, and high chance of being inactiv

Inactive Publication Date: 2011-10-13
F STAR BIOTECHNOLOGISCHE FORSCHUNGS & ENTWICKLUNGS GMBH
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

There is stringent “quality control” in the cells which prevent the Immunoglobulin from being secreted unless it is properly folded, and altering the amino acid sequence of the loop might cause the protein to fold into a structure which the cell would detect as incorrect, and hence degrade it.
Thus, besides the examples shown it was considered to be difficult to further modify the structural loops without changing the nature of the Immunoglobulin.
Nevertheless every peptide grafted into a non-CDR loop according to this disclosure has a high chance of being inactive by the different structural environment it has been selected.

Method used

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  • Synthetic immunoglobulin domains with binding properties engineered in regions of the molecule different from the complementarity determining regions
  • Synthetic immunoglobulin domains with binding properties engineered in regions of the molecule different from the complementarity determining regions
  • Synthetic immunoglobulin domains with binding properties engineered in regions of the molecule different from the complementarity determining regions

Examples

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example 1

Construction of the CH3 Library and Phage Surface Display

[0252]The crystal structure of an IgG1 Fc fragment, which is published in the Brookhaven Database as entry 1OQO.pdb was used to aid in the design of the mutated CH3 domain.

[0253]The sequence which was used as the basis for construction of the CH3 library is given in SEQ ID No. 1. In this sequence, the first amino acid corresponds to Proline 343 of chain A of Brookhaven database entry 1oqo.pdb. The last residue contained in 1oqo.pdb is Serine 102 of SEQ ID No. 1. After detailed analysis of the structure of 1oqo.pdb and by visual inspection of the residues forming the loops which connect the beta strands, it was decided to randomize residues 17, 18 and 19, which are part of the loop connecting beta strand A-B as well as 71, 72, 73, 76, and 77, which are part of the loop connecting beta strand E-F of SEQ ID No. 1. A molecular model of the engineered CH3 domain, with the randomized part indicated by a solvent accessible surface is...

example 2

Construction of the CH3+3 Library

[0255]This library was constructed and cloned in the same way as the CH3 library. The amino acid sequence of the construct is given in SEQ ID No. 10, the corresponding nucleotide sequence in SEQ ID No. 11, and the primers used for construction were SEQ ID No. 4-7, SEQ ID No. 9 and SEQ ID No. 12.

example 3

Construction of the CH3+5 Library

[0256]This library was constructed and cloned in the same way as the CH3 library. The amino acid sequence of the construct is given in SEQ ID No. 13, the corresponding nucleotide sequence in SEQ ID No. 14, and the primers used for construction were SEQ ID No. 4-7, SEQ ID No. 9 and SEQ ID No. 15.

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Abstract

Immunoglobulins which each have one or more amino acid modifications in at least one structural loop region of such immunoglobulins, where the modified loop region specifically binds to an epitope of an antigen to which an unmodified immunoglobulin does not significantly bind, obtained from display libraries.

Description

CROSS-REFERENCE TO RELATED APPLICATIONS[0001]This application is a continuation of and claims the benefit of priority from U.S. patent application Ser. No. 13 / 149,871, filed on May 31, 2011, which is a continuation of and claims the benefit of priority from U.S. patent application Ser. No. 11 / 722,517, filed on Jun. 21, 2007, which is the U.S. national phase under 35 U.S.C. §371 of PCT International Application No. PCT / EP2006 / 050059, filed on Jan. 5, 2006, which claims the benefit of priority under 35 U.S.C. 119(e) to U.S. Provisional Patent Application No. 60 / 641,144, filed on Jan. 5, 2005. The entire contents of the foregoing patent applications are incorporated herein by reference in their entireties.INCORPORATION-BY-REFERENCE OF MATERIAL SUBMITTED ELECTRONICALLY[0002]The entire content of a Sequence Listing titled “SEQUENCE_LISTING.txt,” created on Jun. 1, 2011 and having a size of 62 kilobytes, which has been submitted in electronic form in connection with the present applicatio...

Claims

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Application Information

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IPC IPC(8): C07K16/00
CPCC07K16/00C07K2317/21C07K2318/20C07K2317/526C07K2317/52C07K19/00C07K2319/30A61P31/00A61P33/02A61P35/00A61P37/02A61P37/08C12N15/62C40B40/10C40B40/08C07K16/28C07K16/40C07K2317/31C07K2317/522C07K2317/55
Inventor RUKER, FLORIANHIMMLER, GOTTFRIEDWOZNIAK-KNOPP, GORDANA
Owner F STAR BIOTECHNOLOGISCHE FORSCHUNGS & ENTWICKLUNGS GMBH
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