Abstract:
The present invention relates to a method for suppressing aggregation of polypeptide. Specifically, the present invention relates to a method for suppressing, in a solution comprising an antibody or an Fc region-containing protein, formation of an aggregate derived from an antibody or an Fc region-containing protein having a non-native conformation, the method comprising: the steps of (i) binding an AF.2A1 polypeptide or an analog thereof with an aggregate derived from the antibody or Fc region-containing protein having a non-native conformation in the solution; and (ii) collecting the aggregate bound to the polypeptide or analog thereof from the solution.
Abstract:
Polypeptides which have binding activity to an Fc region of immunoglobulin G and can be favorably used in detecting, purifying, immobilizing or removing an antibody, immunoglobulin G or a protein containing an Fc region of immunoglobulin G, are described. Methods for detecting, purifying, immobilizing or removing an antibody, immunoglobulin G or a protein containing an Fc region of immunoglobulin G, by using the peptide, are also described.
Abstract:
The purpose of the present invention is to provide a method for producing a very stable, cyclized mutant protein such that high cyclization efficiency is achieved while the number of amino acids added is minimal and the biological properties of an original protein are maintained. In view of conformational information about the original protein, secondary structure-free regions at N/C terminal portions are deleted. Then, a protein database is screened for proteins with secondary structures similar to those of N/C terminal residues of a secondary structure-forming portion after the deletion. The screening results are used to determine the amino acid length of a loop structure through which the N-terminus and the C-terminus of the secondary structure-forming portion of the original protein are to be connected. A cyclized mutant protein is finally produced having a loop structure with the determined amino acid length.
Abstract:
The present invention relates to a novel polypeptide having affinity for proteins partially including a CH1-CL domain forming a non-native three-dimensional structure and capable of being suitably used for detecting, immobilizing, or removing these proteins and relates to use of the polypeptide. Specifically, disclosed are a polypeptide consisting of an amino acid sequence represented by any one of the following formulas 1 to 3: (1) P-Q-x-I-x-L-x-[IL]-[NT]-[YW] (SEQ ID NO: 1), (2) Y-D-P-E-T-G-T-W-P-Q-x-I-x-L-x-[IL]-[NT]-[YW] (SEQ ID NO: 4), and (3) P-N-S-G-G-G-G-S-Y-D-P-E-T-G-T-W-P-Q-x-I-x-L-x-[IL]-[NT]-[YW] (SEQ ID NO: 7) (wherein x represents an amino acid residue; and brackets represent any one of the amino acid residues within the brackets), and a method of using the polypeptide to detect, purify, or remove a protein partially including a CH1-CL domain forming a non-native three-dimensional structure.
Abstract:
The purpose of the present invention is to provide a method for producing a very stable, cyclized mutant protein such that high cyclization efficiency is achieved while the number of amino acids added is minimal and the biological properties of an original protein are maintained. In view of conformational information about the original protein, secondary structure-free regions at N/C terminal portions are deleted. Then, a protein database is screened for proteins with secondary structures similar to those of N/C terminal residues of a secondary structure-forming portion after the deletion. The screening results are used to determine the amino acid length of a loop structure through which the N-terminus and the C-terminus of the secondary structure-forming portion of the original protein are to be connected. A cyclized mutant protein is finally produced having a loop structure with the determined amino acid length.
Abstract:
Disclosed is a molecular library comprising a group of a plurality of molecules, wherein each member of the library is a polypeptide having a randomized sequence moiety and a microprotein moiety. The microprotein is a protein comprising an amino acid sequence of 30 or less amino acid residues having the ability to form a particular conformation by spontaneous folding in a solution and is, for example, chignolin comprising the amino acid sequence represented by SEQ ID NO: 1. Also, disclosed is a method for identifying a novel functional molecule using the library of the present invention.
Abstract:
The present invention relates to a method for suppressing aggregation of polypeptide. Specifically, the present invention relates to a method for suppressing, in a solution comprising an antibody or an Fc region-containing protein, formation of an aggregate derived from an antibody or an Fc region-containing protein having a non-native conformation, the method comprising: the steps of (i) binding an AF.2A1 polypeptide or an analog thereof with an aggregate derived from the antibody or Fc region-containing protein having a non-native conformation in the solution; and (ii) collecting the aggregate bound to the polypeptide or analog thereof from the solution.
Abstract:
The purpose of the present invention is: to provide an excellent protein which is further reduced in the binding property to an Fc region of an immunoglobulin and/or the binding property to an Fab region of the immunoglobulin in a weakly acidic region compared with that of a protein containing an extracellular domain of wild-type protein G, and which still keeps a high antibody-binding activity in a neutral region; and to capture and collect an antibody readily using the protein without denaturating the antibody. The present invention relates to: a protein that is reduced in the binding property to an Fc region of an immunoglobulin and/or the binding property to an Fab region of the immunoglobulin in a weakly acidic region compared with that of a multimer comprising an extracellular domain of wild type one, which is a domain having a binding activity to a protein comprising an Fc region of immunoglobulin G, while keeping a high antibody-binding activity in a neutral region, and also has a binding activity to a protein comprising the Fc region of immunoglobulin G, wherein the protein comprises a tandem-type multimer of a mutant of the extracellular domain; and others.
Abstract:
The purpose of the present invention is to provide a method for producing a very stable, cyclized mutant protein such that high cyclization efficiency is achieved while the number of amino acids added is minimal and the biological properties of an original protein are maintained. In view of conformational information about the original protein, secondary structure-free regions at N/C terminal portions are deleted. Then, a protein database is screened for proteins with secondary structures similar to those of N/C terminal residues of a secondary structure-forming portion after the deletion. The screening results are used to determine the amino acid length of a loop structure through which the N-terminus and the C-terminus of the secondary structure-forming portion of the original protein are to be connected. A cyclized mutant protein is finally produced having a loop structure with the determined amino acid length.