BDB -BiopanningDataSet Details

Biopanning Data

BiopanningDataSet ID: 1705

Peptides:

Sequences	Affinity Values
VRRSKHGARKDR	[191]

Sequences Features:

Motif:

Unique Sequence Number:

Experimental Method:

Bacterial display (common panning)

Sequencing Platform:

Sequencing Method:

Sanger sequencing

Rounds of Panning:

Reference:

PMID: 19048606

Target Name:

Heparin

Template Name:

Not determined.

Structure of Target-Template Complex:

Not determined.

Structure of Target-Peptide Complex:

Not determined.

Library Name:

FliTrx bacterial display library (X12)

Affinity Measurement Method:

Surface plasmon resonance (SPR)

Affinity Measurement Description:

The evaluation of the kinetic parameters was performed using a SPR-based BIAcoreX biosensor (BIAcore). The dissociation constant (KD =kd/ka, nm) is shown.

Brief Description:

BiopanningDataSet Comments:

Isolated insert analysis revealed a novel heparin-binding peptide sequence, VRRSKHGARKDR, designated as HBP12. Our analysis of the sequence alignment of heparin-binding motifs known as the Cardin-Weintraub consensus (BBXB, where B is a basic residue) indicates that the HBP12 peptide sequence contains two consecutive heparin-binding motifs (i.e. RRSK and RKDR). SPR-based BIAcore technology demonstrated that the HBP12 peptide binds to heparin with high affinity (K(D) = 191 nM). The HBP12 peptide is found to bind the cell surface HS expressed by osteoblastic MC3T3 cells and promote HS-dependent cell adhesion. Moreover, the surface-immobilized HBP12 peptide on titanium substrates shows significant increases in the osteoblastic MC3T3-E1 cell adhesion and proliferation.

Curator:

Curation Date:

0000-00-00

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