BDB -BiopanningDataSet Details

Biopanning Data

BiopanningDataSet ID: 3246

Peptides:

Sequences	Affinity Values
DSQFNKYSIATV(2/19) VQCRLGPPWCAK(1/19) SLLHTSMPSMIA(1/19) KVEPGTGAHSWQ(1/19) VADSNWINPRGS(1/19) QGPHEHTKIHID(1/19)	[0.60] [1.32] [0.57] [0.55] [0.52] [0.41]

Sequences Features:

Motif:

Unique Sequence Number:

Experimental Method:

Phage display (common panning)

Sequencing Platform:

Sequencing Method:

Sanger sequencing

Rounds of Panning:

Reference:

PMID: 28780344

Target Name:

Cholera toxin subunit B, CTX-B

Template Name:

Not determined.

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

Affinity Measurement Description:

ELISA signal was measured at 405nm using a microplate spectrophotometer (Multiskan FC, Thermo Scientiﬁc, Waltham, MA, USA). Binding affinity values shown were regenerated from Figure 1A.

Brief Description:

BiopanningDataSet Comments:

Biopanning over recombinant CTX-B led to rapid screening of a unique peptide with an amino acid sequence of VQCRLGPPWCAK, and the phage-displayed peptides analyzed using ELISA, were found to show specific affinities towards CTX-B. To address the use of affinity peptides in development of the biosensor, sequences of newly selected peptides were modified and chemically synthesized to create a series of affinity peptides.Performance of the biosensor was studied using plasmonic-based optical techniques: localized surface plasmon resonance (LSPR) and surface-enhanced Raman scattering (SERS). The limit of detection (LOD) obtained by LSPR with 3σ-rule was 1.89ng/mL, while SERS had a LOD of 3.51pg/mL. In both cases, the sensitivity was much higher than the previously reported values, and our sensor system was specific towards actual CTX-B secreted from V. cholera, but not for CTX-AB5.

Curator:

Yewei Fang

Curation Date:

2017-10-24

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