BDB -BiopanningDataSet Details

Biopanning Data

BiopanningDataSet ID: 560

Peptides:

Sequences	Affinity Values
SAMWDF(3) SFIWDF(2) TNMWDF(2) ITMWDF(2) SDWWDF(1)	[2.4 ± 0.13, 1.82 ± 0.09] [2.1 ± 0.15, 1.70 ± 0.10] [2.05 ± 0.12, 1.42 ± 0.08] [2.2 ± 0.13, 1.36 ± 0.06] [2.1 ± 0.10, 1.48 ± 0.12]

Sequences Features:

Motif:

[ST]-x(2)-W-D-F

Unique Sequence Number:

Experimental Method:

Phage display (common panning)

Sequencing Platform:

Sequencing Method:

Sanger sequencing

Rounds of Panning:

Reference:

PMID: 19118103

Target Name:

Anti-hCXCR1 monoclonal antibody 5A12

Template Name:

C-X-C chemokine receptor type 1, CXC-R1, CXCR-1

Structure of Target-Template Complex:

Not determined.

Structure of Target-Peptide Complex:

Not determined.

Library Name:

fdMED1-based X6 phage display library

Affinity Measurement Method:

ELISA

Affinity Measurement Description:

ELISA was used to test the reactivity of mAb 5A12 with phage-peptide clones and the corresponding synthesized peptides, respectively. For phage ELISA, the absorbance was measured at 450 nm (A450 nm). Data shown are A450nm after substraction of background. For peptide ELISA, the absorbance was measured at 450 nm (A450 nm). As control, the linear hexapeptide MRFIAW was used. Data shown were reproduced from the graph. The A450 of MRFIAW is 0.06.

Brief Description:

BiopanningDataSet Comments:

The phage bearing the peptides showed specific binding to immobilized mAb 5A12. In FACScan analysis, all selected phage peptides were able to strongly inhibit the binding of mAb 5A12 to hCXCR1-transfected preB 300-19 murine cells. Furthermore, synthetic peptides of the corresponding phage epitopes were effective in blocking the antibody-CXCR1 interactions and to inhibit the binding of hCXCL8 to hCXCR1 transfectants. In vivo, SAMWDF blockade hCXCL8-induced neutrophil recruitment in skin inflammation in rabbits.

Curator:

Curation Date:

0000-00-00

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