BDB -BiopanningDataSet Details

Biopanning Data

BiopanningDataSet ID: 1765

Peptides:

Sequences

Affinity Values

EPYGFIAFSRAAHSP(4)
ARLSPTMVHPNGAQP(2)
TFFQVPPRILVGSAS(1)
ARLGSVLISSGPSSD(1)
GRPPDSVFRSRGWLS(1)
AWRNMIRYGVDLPAF(1)

[0.563 ± 0.310]
[1.268 ± 0.179]
[0.170 ± 0.201]
[0.261]
[0.891 ± 0.280]
[0.323 ± 0.092]

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:

6' ganglioside GM3

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, clones f1 (displaying ARLSPTMVHPNGAQP), f9 (displaying EPYGFIAFSRAAHSP) and f12 (displaying GRPPDSVFRSRGWLS) were found to have a high affinity by SPR analysis, with dissociation constant (Kd) values of 7.8-30nM 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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