BDB -BiopanningDataSet Details

Biopanning Data

BiopanningDataSet ID: 3249

Peptides:

Sequences	Affinity Values
KVVKTHR MVYLTEK KTVLTHR NAGHLSQ NMHTPMV	[1.34] [0.49] [0.28] [0.20] [0.18]

Sequences Features:

Motif:

Unique Sequence Number:

Experimental Method:

Phage display (subtractive panning)

Sequencing Platform:

Sequencing Method:

Sanger sequencing

Rounds of Panning:

Reference:

PMID: 28744632

Target Name:

Template Name:

Tumor necrosis factor ligand superfamily member 10

Structure of Target-Template Complex:

Not determined.

Structure of Target-Peptide Complex:

Not determined.

Library Name:

Ph.D.-C7C phage display library (CX7C)

Affinity Measurement Method:

ELISA

Affinity Measurement Description:

Absorbance at 450 nm was measured on a Tecan microplate spectrophotometer (Genios). Data shown were regenerated from Figure 2b.

Brief Description:

For phage selection, phage particles were pre-incubated with mouse Fc. Then, bound phages were removed using magnetic beads with immobilized protein G (Invitrogen), while the supernatant was used for further selection of more specific peptides by adding mouse DR5-Fc.

BiopanningDataSet Comments:

The cyclopeptide sequences selected from the library show appreciable homology at positions 2 (valine), 4 (leucine), and 5 (tyrosine). Substitution of valine for threonine in position 2 in a KVVLTHR peptide leads to a decrease in binding. It is possible that these very amino acids play the key role in interaction between the peptide and DR5.

Curator:

Yewei Fang

Curation Date:

2017-10-24

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