Supramolecular high affinity protein-binding system for purification of biomacromolecules
AssigneesThe Johns Hopkins University, Bristol-Myers Squibb Company
InventorsHonggang Cui, Yi Li, Xuankuo Xu, Lye Lin Lock, Zhengjian Li
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Abstract
In certain embodiments, the present invention provides novel antibody purification methods and systems using a potentially simple and cost-efficient means. In some embodiments, customized Z-33 derived from Staphylococcus aureus Protein A is used to construct immuno-amphiphile molecules which can assemble into immunofibers in aqueous solution with bioactive epitopes on the surface and have IgG binding ability.
Claims6
An immuno-amphiphile comprising an antibody binding peptide conjugated to a linear hydrocarbon chain.
An immuno-amphiphile comprising an antibody binding peptide conjugated to a linear hydrocarbon chain and wherein the peptide has an α-helical conformation when in an aqueous solution at physiological pH.
An immuno-amphiphile comprising an antibody binding peptide conjugated to a linear hydrocarbon chain, wherein the antibody binding peptide has a hydrophilic amino acid sequence of the Z33 peptide of Protein A of Staphylococcus aureus, or a functional portion or fragment or derivative thereof.
An immuno-amphiphile comprising an antibody binding peptide conjugated to a linear hydrocarbon chain, wherein the antibody binding peptide has the amino acid sequence FNMQQQRRFYEALHDPNLNEEQRNAKIKSIRDD (SEQ ID NO:
- 1), or a functional portion or fragment or derivative thereof.
Dependencies are inferred from the claim text.