BDB -BiopanningDataSet Details

Biopanning Data

BiopanningDataSet ID: 574

Peptides:

Sequences

Affinity Values

SWELYYPLRANL(8)
QWEIRYPWPSMG(4)
QWTYYLPLTPRW(2)
EWTYTFPTAHSI(2)
EWFWSWPGYSNT(1)
SWEWYIPYLNRT(1)
AWTWSLPTLPQS(1)

[+, +, -][9.4, 0.323]
[+, +, -][NT]
[+, +, -][NT]
[+, +, -][NT]
[+, +, -][NT]
[+, +, -][NT]
[+, +, -][NT]

Sequences Features:

Motif:

Unique Sequence Number:

Experimental Method:

Phage display (common panning)

Sequencing Platform:

Sequencing Method:

Sanger sequencing

Rounds of Panning:

Reference:

PMID: 19465078

Target Name:

Cadherin-1

Template Name:

Cadherin-1

Structure of Target-Template Complex:

Not determined.

Structure of Target-Peptide Complex:

Not determined.

Library Name:

Ph.D.-12 phage display library (X12)

Affinity Measurement Method:

ELISA,Surface plasmon resonance (SPR)

Affinity Measurement Description:

The binding of each clone to E-cad/Fc chimeric protein, N-cad/Fc chimeric protein and VE-cad/Fc chimeric protein was conﬁrmed by ELISA, respectively. + denotes phage clone bound to the cadherin ectodomain/Fc chimeric protein and - represents phage clone did not bind to the cadherin ectodomain/Fc chimeric protein. Besides, the binding of the linear peptide, H-SWELYYPLRANL-NH2 to E-, N-, P- and OB-cad/Fc chimeric proteins was analyzed by SPR. The linear peptide, H-SWELYYPLRANL-NH2 was found to bind to the E- and N-cad/Fc chimeric proteins with high affinities (Kd, μM) of 9.4 μM and 0.323 μM, respectively. NT denotes not tested.

Brief Description:

In fact, the target used in the experiment is a chimeric protein composed of the E-cadherin ectodomain fused to the immunoglobulin G1 Fc fragment. The bound phages were eluted through using 0.2M glycine HCl, pH 2.2 followed by neutralization with 1 M Tris-HCl, pH 9.1. Total number of clones were 24.

BiopanningDataSet Comments:

All of the phage clones not only bound to the E-cad/Fc chimeric protein, but also to the Ncad/Fc chimeric protein. Peptide SWELYYPLRANL was found to bind both E- and N-cad/Fc chimeric proteins with affinities (KD) of 9.4 μM and 323 nM, respectively, as judged by surface plasmon resonance spectroscopy.

Curator:

Curation Date:

0000-00-00

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