Mutated immunoglobulin-binding protein
AssigneeCytiva BioProcess R&D AB
InventorSophia Hober
Life of this patent
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Abstract
The present invention relates to an immunoglobulin-binding protein, wherein at least one asparagine residue has been mutated to an amino acid other than glutamine or aspartic acid, which mutation confers an increased chemical stability at pH-values of up to about 13-14 compared to the parental molecule. The protein can for example be derived from a protein capable of binding to other regions of the immunoglobulin molecule than the complementarity determining regions (CDR), such as protein A, and preferably the B-domain of Staphylococcal protein A. The invention also relates to a matrix for affinity separation, which comprises an immunoglobulin-binding protein as ligand coupled to a solid support, in which protein ligand at least one asparagine residue has been mutated to an amino acid other than glutamine.
Claims13
A matrix for affinity chromatography, comprising a plurality of ligands coupled to a solid support,
- wherein the ligands comprise an immunoglobulin-binding protein, or multimer thereof that binds to other regions of the immunoglobulin molecule than the complementarity determining regions (CDR), and
- wherein at least one of N23 and N43 of a parental immunoglobulin-binding protein defined by SEQ ID NOS:1 or 2 have been mutated to amino acid residues selected from A, I, S, T, E, or H,
- wherein the N23 and N43 asparagine residues can be mutated to amino acid residues that are the same or different from each other, and
- wherein the mutations have conferred an increased chemical stability at alkaline pH-values compared to the parental immunoglobulin-binding protein.
Dependencies are inferred from the claim text.