BDB -BiopanningDataSet Details

Biopanning Data

BiopanningDataSet ID: 1764

Peptides:

Sequences

Affinity Values

ARLSPTMVHPNGAQP(2)
GLAYSRFKVSRAIWR(2)
HRWMPHVFAVRQGAS(1)
ALADSIWSSRSGPGL(1)
KDFLSGLRHLHFLHS(1)
TFRLPLVRAQYDSSH(1)
ARVMRQVCGGTGCGV(1)
TSVNRGFLLQRASHP(1)

[1.268 ± 0.179]
[0.283]
[0.319 ± 0.078]
[0.310 ± 0.136]
[0.319 ± 0.122]
[0.139]
[0.270 ± 0.201]
[0.192]

Sequences Features:

Motif:

Unique Sequence Number:

Experimental Method:

Phage display (competitive panning)

Sequencing Platform:

Sequencing Method:

Sanger sequencing

Rounds of Panning:

Reference:

PMID: 20476787

Target Name:

Hemagglutinin, HA

Template Name:

Sialyl Lewis(X), SLX

Structure of Target-Template Complex:

Not determined.

Structure of Target-Peptide Complex:

Not determined.

Library Name:

X15 fUSE5 phage display library

Affinity Measurement Method:

ELISA,Surface plasmon resonance (SPR)

Affinity Measurement Description:

In phage ELISA, the absorbance at 492 nm was determined. Data shown were reproduced from the graph and expressed as means ± the standard deviation (n = 3). Besides, clone f1 (displaying ARLSPTMVHPNGAQP) was found to have a high affinity by SPR analysis, with dissociation constant (Kd) values of 7.8 and 8.6 nM against H1 and H3.

Brief Description:

BiopanningDataSet Comments:

A docking simulation suggested that, similar to sialic acid, the peptides are recognized by the receptor-binding site in HA, which indicates that these peptides mimic the sialic acid structure. N-stearoyl peptides inhibited infections by the A/Puerto Rico/8/34 (H1N1) and A/Aichi/2/68 (H3N2) strains of influenza virus. Such HA-inhibitors are promising candidates for novel antiviral drugs.

Curator:

Curation Date:

0000-00-00

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