BDB -BiopanningDataSet Details

Biopanning Data

BiopanningDataSet ID: 1658

Peptides:

Sequences

FPRWKLLAHWADRWWF(5)
MHYEAVRVGRVLRFLA(4)
IRMMVSFLRRQSRWWL(1)
ARVFGLWLRSMSDMWL(1)
MWVHSAAMATGLASRM(1)
GNRWQYWIAFRMRYVA(1)
RHLLLVDRLRAIALLL(1)
RVLRYYLVGLALRQMA(1)
AAVASMLRHLAGLFVL(1)
FPRWKLLAHWADRGWC(1)
FPRWKLLAHWADRWWV(1)
FLRWKLLAHWADRWWF(1)
SQRSTMYIAAVLRWLA(1)
MVPSWVGLARVLRWLA(1)
LVLLGRMLKFVA(1)

Sequences Features:

Motif:

Unique Sequence Number:

Experimental Method:

mRNA display (common panning)

Sequencing Platform:

Sequencing Method:

Sanger sequencing

Rounds of Panning:

Reference:

PMID: 20181936

Target Name:

B-cell lymphoma/leukemia 10

Template Name:

Not determined.

Structure of Target-Template Complex:

Not determined.

Structure of Target-Peptide Complex:

Not determined.

Library Name:

X16 mRNA display library

Affinity Measurement Method:

Fluorescence polarization

Affinity Measurement Description:

To evaluate the affinity of the selected peptides for the BH3-recognition site of Bcl-XL, competition fluorescence polarization assay was performed. The selected peptide A10 (FPRWKLLAHWADRWWF) (IC50=0.9 μM) showed marked inhibitory activity.

Brief Description:

BiopanningDataSet Comments:

The selected peptides have sequence similarity with the Bcl-2 family BH3 domains, and one of them (FPRWKLLAHWADRWWF) has higher affinity (IC 50 = 0.9 μM) than Bak BH3 (IC 50 = 11.8 μM) for Bcl-X(L) in vitro. We also found that GFP fusions of the selected peptides specifically interact with Bcl-X(L), localize in mitochondria, and induce cell death. Further, a chimeric molecule, in which the BH3 domain of Bak protein was replaced with a selected peptide, retained the ability to bind specifically to Bcl-X(L). These results demonstrate that this selected peptide specifically antagonizes the function of Bcl-X(L) and overcomes the effects of Bcl-X(L) in intact cells.

Curator:

Curation Date:

0000-00-00

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