BDB -BiopanningDataSet Details

Biopanning Data

BiopanningDataSet ID: 3497

Peptides:

Sequences

Affinity Values

HSFKWLDSPRLR(5)
GAYTSWRTSTNA(3)
DLVSWAGSGKKH(3)
VHWDFRQWWQPS(1)
AHAHTNWTSWWE(1)
ADWYHWRSHSSS(1)
IPNYSMQSREYR(1)
HYRPFTQEHRVT(1)
HSFKGWDWPRLR(1)
GWKSHEPKGHGS(1)
EHLHASWNFSSG(1)
YDVPNKSWRTSW(1)

[2.580765±0.716041]
[1.788102±0.130236]
[1.855382±0.037913]
[2.125573±0.006749]
[2.594787±0.006743]
[2.043153±0.005618]
[2.080793±0.006749]
[3.67144]
[2.795317±0.006743]
[2.694727±0.005618]
[1.808223±0.006743]
[4.17569]

Sequences Features:

Motif:

Unique Sequence Number:

Experimental Method:

Phage display (subtractive panning)

Sequencing Platform:

Sequencing Method:

Sanger sequencing

Rounds of Panning:

Reference:

PMID: 31888393

Target Name:

AdipoR-12C

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 OD405 was measured using a microplate reader (StatFax-2100, Awarness Technology, Fisher Bioblock Scientific, Tournai, Belgium). Data (OD405) shown were reproduced from Figure 1G in the reference.

Brief Description:

Bovine serum albumin (BSA) immobilized on Dynabeads was used as control protein during the preselection steps of the 3 panning rounds to exclude non-specific phages.

BiopanningDataSet Comments:

The selected peptide P17 (IPNYSMQSREYR) recognizes AdipoR1/R2 expressed by skeletal muscle, liver and pancreatic islets. In HepaRG and C2C12 cells, P17 induced the activation of AMPK (AMPKα-pT172) and the expression of succinate dehydrogenase and glucokinase; no cytotoxic effects were observed on HepaRG cells. In db/db mice, P17 promoted body weight and glycemia stabilization, decreased plasma triglycerides to the range of healthy mice and increased adiponectin (in high fat-fed mice) and insulin (in chow-fed mice) levels. It restored to the range of healthy mice the tissue levels and subcellular distribution of AdipoR1/R2, AMPKα-pT172 and PPARα-pS12. In liver, P17 reduced steatosis and apoptosis. The docking of P17 to AdipoR is reminiscent of the binding mechanism of adiponectin. To conclude, we have developed an AdipoR1/AdipoR2-targeted peptide that modulates adiponectin signalling pathways and has therapeutic relevance for T2D and obesity associated pathologies.

Curator:

Chunchao Pu

Curation Date:

2020-12-29

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