BDB -BiopanningDataSet Details

Biopanning Data

BiopanningDataSet ID: 1843

Peptides:

Sequences
CLLGTRWPC CFMESVGRC CLTPEFHIC CLAVGEVLC CFVSPPVGC CMPGWEVLC CKRGNSGSC CQRLVGFAC CLQASPNFC CNGSVRSFC CPGFGLAYC CFLFTFEAC CRGVLMRYC CRAFVVASC CQSHSAFVC

Sequences Features:

Motif:

Unique Sequence Number:

Experimental Method:

Phage display (subtractive panning)

Sequencing Platform:

Sequencing Method:

Sanger sequencing

Rounds of Panning:

Reference:

PMID: 21829599

Target Name:

Human thymic CD4+CD25+ T cells

Template Name:

Not determined.

Structure of Target-Template Complex:

Not determined.

Structure of Target-Peptide Complex:

Not determined.

Library Name:

fUSE5-based CX7C phage display library

Affinity Measurement Method:

Affinity Measurement Description:

Brief Description:

Screening of the phage library was performed by the BRASIL method, which allows the separation of cell-bound from unbound phage in one step. CD4+CD25- cells were used for preclearing.

BiopanningDataSet Comments:

Among the phages sequenced a specific phage peptide for further analysis due to its sequence similarity to the Vitamin D receptor (VDR). This was the first choice because although Vitamin D has been extensively reported to display immunoregulatory functions in different contexts, its role has not been well-defined for human thymic T regs, opening an interesting area for research. The results from the ELISA assay showing that VDR phage was able to bind to active Vitamin D strongly supports our hypothesis. When phages were preincubated with Vitamin D we did not observe binding to VDR, confirming that the peptide, in fact, mimic the Vitamin D binding pocket in VDR and is able to prevent Vitamin D from binding to its native receptor.

Curator:

Curation Date:

0000-00-00

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