BDB -BiopanningDataSet Details

Biopanning Data

BiopanningDataSet ID: 3459

Peptides:

Sequences

Affinity Values

ITMSVPAHNAKE(39/169)
TNTSWDPQYNPD(11/169)
NHFVPTSNRFNA(11/169)
NFTINGKTHRLW(6/169)
NAITLLSPPLHK(5/169)
SSHNHDSYHGTK(2/169)
LMNPATMKTSSG(1/169)
TNTSWDPQYNPD(1/169)
SNMKPSMEYSSR(1/169)
IGNSWPLTSHSW(1/169)
SYNTFMYERASK(1/169)
MVHSKASMWPGK(1/169)
KVYAINSWTNYY(1/169)

[34.2 ± 2.11]
[80.1 ± 1.13]
[120 ± 1.23]
[298 ± 1.45]
[57.1 ± 1.77]
[476 ± 2.73]
[360 ± 1.87]
[47.6 ± 2.51]
[273 ± 1.79]
[144 ± 1.1]
[562 ± 1.69]
[690 ± 2.27]
[1200 ± 90.2]

Sequences Features:

Motif:

Unique Sequence Number:

Experimental Method:

Phage display (competitive panning)

Sequencing Platform:

Sequencing Method:

Sanger sequencing

Rounds of Panning:

Reference:

PMID: 31146360

Target Name:

Tubulin alpha chain

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:

The binding affinities of phages were determined by the enzyme-linked immunosorbent assay (ELISA) method with anti-M13 phage antibody. The optical densities were measured at 450 nm with a Biotrak multiwall plate reader (Amersham Bioscience). Kd (pM) was calculated and shown.

Brief Description:

In the final round, bound phages were eluted by addition of a 10 M excess of tubulin alpha chain.

BiopanningDataSet Comments:

One peptide with the sequence of ITMSVPAHNAKEK demonstrated the high inhibitory effect on microtubule formation with a nanomolar range of IC50 values, which were much lower than a well-known chemical inhibitor—benomyl. Based on these results, this peptide can be employed to further develop promising candidates for novel antifungal agents against Phytophthora blight.

Curator:

Lixu Jiang

Curation Date:

2019-08-17

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