Triple-helical polypeptides lacking binding affinity for the Fc domain of immunoglobulin and uses thereof
AssigneeNavigo Proteins GmbH
InventorsErik Fiedler, Ulrich Haupts, Madlen Zwarg
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Abstract
The present invention relates to the field of protein engineering and purification and relates in particular to novel polypeptides having a triple-helical structure and lacking binding affinity for the Fc domain of immunoglobulin. The invention further relates to uses of the novel non-Fc binding polypeptides in technical applications such as affinity chromatography, as well as in therapy and diagnostics. In addition, the present invention relates to a method of reducing the binding affinity of a polypeptide having a triple-helical structure for the Fc domain of immunoglobulin.
Claims8
A polypeptide having at least 90% identity to any one of SEQ ID NOs:
- 1-15 and 23-30, wherein the polypeptide comprises:
- a) an acidic amino acid selected from aspartic acid (D) and glutamic acid (E) at the position corresponding to position 13 of SEQ ID NO:
- 1-15 and 23-30;
- and
- b) a basic amino acid selected from any one of arginine (R), lysine (K), and histidine (H) at the position corresponding to position 31 of SEQ ID NOs:
- 1-15 and 23-30,
- and further wherein the polypeptide has no detectable binding affinity for the Fc domain of immunoglobulin as determined by Surface Plasmon Resonance (SPR).
Dependencies are inferred from the claim text.