US 2003/0199671 A1Published application

Binding molecules for Fc-region polypeptides

OwnerIsaac Jesus Rondon, Qi-Long Wu +5inventors

InventorsIsaac Jesus Rondon, Qi-Long Wu, Arthur C. Ley, Mark Stochl, Thomas C. Ransohoff, M. Daniel Potter, Marilou Potter

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Abstract

Binding molecules for detecting or isolating immunoglobulin Fc-region polypeptides are described, together with methods of use thereof. Preferred Fc-region binding polypeptides, recombinant bacteriophage expressing Fc-region binding polypeptides, and separation media exhibiting such polypeptides are particularly disclosed.

Claims42

Dependent claims

An isolated polypeptide comprising an amino acid sequence of the formulae I, II, III or IV:

Z1—X1—X2—X3—X4—W—C—Z2(SEQ ID NO:4);
I.
wherein,
Z1 is a polypeptide of at least 6 amino acids;
X1 is G, H, N, R, or S;
X2 is A, D, E, F, I, M, or S;
X3 is A, I, L, M, or V;
X4 is I, M, T, or V;
Z2 is a polypeptide of at least one amino acid or is absent;
and
Z1 contains at least one cysteine residue such that formation of a disulfide bond with the invariant cysteine residue forms a cyclic peptide of 12 amino acids;
Z1—X—W—Z2—W—Z3(SEQ ID NO:5) II.
wherein,
Z1 is a polypeptide of at least one amino acid or is absent;
X is F or Y;
Z2 is a tripeptide;
and
Z3 is a polypeptide of at least one amino acid;
and
wherein at least two of the polypeptides Z1, Z2, and Z3 contain a cysteine residue, such that formation of a disulfide bond between such cysteine residues forms a cyclic peptide of 7-12 amino acids;
Z1—W—Z2—W—W—Z3(SEQ ID NO:6);
III.
wherein,
Z1 is a polypeptide of at least one amino acid;
Z2 is a tripeptide;
and
Z3 is a polypeptide of at least one amino acid;
wherein at least two of the polypeptides Z1, Z2, and Z3 contain a cysteine residue, such that formation of a disulfide bond between such cysteine residues forms a cyclic peptide of 8-12 amino acids, with the proviso that where Z1 contains a cysteine, then Z2 does not contain a cysteine, and where Z2 contains a cysteine, it is the middle residue of the tripeptide and Z3 also contains a cysteine;
Z1—P—Xl—W—X2—C—X3—X4—X5(SEQ ID NO:7);
IV.
wherein,
Z1 is a polypeptide of at least one amino acid and includes a cysteine residue;
X1 is A, E, R, S, or T;
X2 is F, W, or Y;
X3 is D, E, L, M, or Q;
X4 is H, W, or Y;
X5 is F or Y;
and
wherein the cysteine residue in Z1 and the cysteine residue between X2 and X3 form a cyclic peptide of 10-12 amino acids;
wherein said polypeptide binds an immunoglobulin Fc region.

37 more elements

An isolated polypeptide comprising an amino acid sequence selected from the group consisting of:

35 F-C-N-C-W-G-S-H-E-F-T-F-C-V-D-D (SEQ ID NO:137) P-G-W-C-Y-S-D-I-W-G-F-K-H-F-C-N-L-D (SEQ ID NO:138) D-S-S-C-I-K-H-H-N-K-V-T-C-F-F-P (SEQ ID NO:139) R-W-S-C-W-G-V-W-G-C-V-W-V (SEQ ID NO:140) P-V-D-C-K-H-H-F-W-W-C-Y-W-N (SEQ ID NO:141) S-W-N-C-A-F-H-H-N-E-M-V-W-C-D-D-G (SEQ ID NO:142) Y-W-Y-C-W-F-P-D-R-P-E-C-P-L-Y, (SEQ ID NO:143)
wherein said polypeptide binds an immunoglobulin Fc region.

A recombinant bacteriophage expressing an exogenous polypeptide capable of binding to an immunoglobulin Fc region, said exogenous polypeptide comprising an amino acid sequence of any of the formulae I, II, III or IV:

Z1—X1—X2—X3—X4—W—C—Z2(SEQ ID NO:4);
I.
wherein,
Z1 is a polypeptide of at least 6 amino acids;
X1 is G, H, N, R, or S;
X2 is A, D, E, F, I, M, or S;
X3 is A, I, L, M, or V;
X4is I, M, T, or V;
Z2 is a polypeptide of at least one amino acid or is absent;
and
Z1 contains at least one cysteine residue such that formation of a disulfide bond with the invariant cysteine residue forms a cyclic peptide of 12 amino acids;
Z1—X—W—Z2—W—Z3(SEQ ID NO:5) II.
wherein,
Z1 is a polypeptide of at least one amino acid or is absent;
X is F or Y;
Z2 is a tripeptide;
and
Z3 is a polypeptide of at least one amino acid;
and
wherein at least two of the polypeptides Z1, Z2, and Z3 contain a cysteine residue, such that formation of a disulfide bond between such cysteine residues forms a cyclic peptide of 7-12 amino acids;
Z1—W—Z2—W—W—Z3(SEQ ID NO:6);
III.
wherein,
Z1 is a polypeptide of at least one amino acid;
Z2 is a tripeptide;
and
Z3 is a polypeptide of at least one amino acid;
wherein at least two of the polypeptides Z1, Z2, and Z3 contain a cysteine residue, such that formation of a disulfide bond between such cysteine residues forms a cyclic peptide of 8-12 amino acids, with the proviso that where Z1 contains a cysteine, then Z2 does not contain a cysteine, and where Z2 contains a cysteine, it is the middle residue of the tripeptide and Z3 also contains a cysteine;
Z1—P—X1—W—X2—C—X3—X4—X5(SEQ ID NO:7);
IV.
wherein,
Z1 is a polypeptide of at least one arnino acid and includes a cysteine residue;
X1 is A, E, R, S, or T;
X2 is F, W, or Y;
X3 is D, E, L, M, or Q;
X4 is H, W, or Y;
X5 is F or Y;
and
wherein the cysteine residue in Z1 and the cysteine residue between X2 and X3 form a cyclic peptide of 10-12 amino acids.

36 more elements

Separation media comprising the reaction product of:

(a) an amine-reactive chromatographic matrix material;
and
(b) a polypeptide selected from the group consisting of:
38 Ac-GDDHMCVYTTWGELIWCDNHEPGPEGGGK-NH2;
(SEQ ID NO:144) Ac-AGKYWCSFWGLQCKTGTPGPEGGGK-NH2;
(SEQ ID NO:146) Ac-AGPVDCKHHFWWCYWNGTPGPEGGGK-NH2;
(SEQ ID NO:153) Ac-GDDDHCYWFREWFNSECPHGEPGPEGGGK-NH2;
(SEQ ID NO:154) Ac-GDRRACSRDWSGALVWCAGHEPGPEGGGK-NH2;
(SEQ ID NO:145) Ac-AGYYWCNYWGLCPDQGTPGPEGGGK-NH2;
(SEQ ID NO:155) Ac-AGPHNCDDHYWYCKWFPGPEGGGK-NH2;
(SEQ ID NO:150) Ac-AGSYWCKIWDVCPQSPGPEGGGK-NH2;
(SEQ ID NO:147) Ac-AGKYWCNLWGVCPANPGPEGGGK-NH2;
(SEQ ID NO:148) Ac-AGAATCSTSYWYYQWFCTDSPGPEGGGK-NH2;
(SEQ ID NO:151) Ac-AGTYWCTFWELPCDPAPGPEGGGK-NH2;
(SEQ ID NO:149) Ac-AGYWYCWFPDRPECPLYPGPEGGGK-NH2;
(SEQ ID NO:152) Ac-GDSWVCWKAKWWEDKRCAPFGTPGPEGGGK-NH2;
(SEQ ID NO:156) Ac-GDNPMCWKKSWWEDAYCINHGTPGPEGGGK-NH2;
(SEQ ID NO:157) Ac-GDSWNCAFHHNEMVWCDDGGTPGPEGGGK-NH2;
(SEQ ID NO:158) Ac-GDWGECTVTSYGELIWCGGLEPGPEGGGK-NH2;
(SEQ ID NO:159) Ac-GDNPMCWRASWWEDAYCINHEPGPEGGGK-NH2;
(SEQ ID NO:160) Ac-GDNPMCWRAHWWEDAYCINHEPGPEGGGK-NH2;
(SEQ ID NO:161) Ac-GDDHMCVYTTWGELIWCDNHEPGPEG-X-NH2;
(SEQ ID NO:162) Ac-GDDHMCVYTTWGELPWCDNHEPG-X-Su-X-NH2;
(SEQ ID NO:163) Ac-GDDHMCVYTTWGELIWCDNHEPG-X-Z-X-NH2;
(SEQ ID NO:164) Ac-GDDHMCVYTTWGELIWCDNH-X-NH2;
(SEQ ID NO:165) Ac-GDDHMCVYTTWGELIWCDNH-X-Su-X-NH2;
(SEQ ID NO:166) Ac-GDDHMCVYTTWGELIWGDNH-X-Z-X-NH2;
(SEQ ID NO:167) Ac-DHMCVYTTWGELIWCDNHEPGPEGGGK-NH2;
(SEQ ID NO:169) Ac-EHMCVYTTWGELTWCDNHEPGPEGGGK-NH2;
(SEQ ID NO:170) Ac-ACVYTTWGELTWCDNHEPGPEGGGK-NH2;
(SEQ ID NO:171) Ac-TCVYTTWGELIWCDNHEPGPEGGGK-NH2;
(SEQ ID NO:172) Ac-ECVYTTWGELTWCDNHEPGPEGGGK-NH2;
(SEQ ID NO:173) Ac-VCVYTTWGELIWCDNHEPGPEGGGK-NH2;
(SEQ ID NO:174) Ac-[Nle]CVYTTWGELIWCDNHEPGPEGGGK-NH2;
(SEQ ID NO:175) Ac-CVYTTWGELIWCDNHEPGPEGGGK-NH2;
(SEQ ID NO:176) Ac-SRACSRDWSGALVWCAGHEPGPEGGGK-NH2;
(SEQ ID NO:177) Ac-RRACSRDWSGALVWCAGHEPGPEGGGK-NH2;
(SEQ ID NO:178) Ac-ERACSRDWSGALVWCAGHEPGPEGGGK-NH2;
(SEQ ID NO:179) Ac-ACSRDWSGALVWCAGHEPGPEGGGK-NH2;
(SEQ ID NO:180) Ac-TCSRDWSGALVWCAGHEPGPEGGGK-NH2;
(SEQ ID NO:181) Ac-ECSRDWSGALVWCAGHEPGPEGGGK-NH2;
(SEQ ID NO:182) Ac-VCSRDWSGALVWCAGHEPGPEGGGK-NH2;
(SEQ ID NO:183) Ac-GCSRDWSGALVWCAGHEPGPEGGGK-NH2;
(SEQ ID NO:184) and Ac-CSRDWSGALVWCAGHEPGPEGGGK-NH2, (SEQ ID NO:185)
wherein:
Ac-denotes N-terminal acetylation;
—NH2 denotes C-terminal amidation;
[Nle] denotes norleucine;
—X—NH2 dentoes the C-terminal group —NH—(CH2CH2O)2—CH2CH2—NH2;
—X—Su—X—NH2 denotes the C-terminal group —NH—(CH2CH2O)2—CH2CH2—NH—C:O—CH2CH2—C:O—NH—(CH2CH2O)2—CH2CH2—NH2;
and —X—Z—X—NH2 denotes the C-terminal group —NH—(CH2CH2O)2—CH2CH2—NH—C:O—CH2—O—(CH2CH2O)2—CH2—C:O—NH—(CH2CH2O)2—CH2CH213 NH2.

48 more elements

Dependencies are inferred from the claim text.

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Abstract