Evidence map›Paper›PMID 29912982›Full record

ArticlePloS one2018

Discovery of a novel potent peptide agonist to adiponectin receptor 1.

Sunghwan Kim, Younho Lee, Jun Woo Kim, Young-Jin Son, Min Jung Ma, Jee-Hyun Um, Nam Doo Kim, Sang Hyun Min, Dong Il Kim, Brian B Kim

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
3.2field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 42 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 5 institutions in 1 country.

Sunghwan KimNew Drug Development Center, Daegu-Gyeongbuk Medical Innovation Foundation, Daegu, South Korea.ORCID 0000-0002-1927-9617
Younho LeeCollege of Pharmacy and Yonsei Institute of Pharmaceutical Sciences, Yonsei University, 85 Songdogwahak-ro, Yeonsu-gu, Incheon, South Korea.ORCID 0000-0002-4235-1269
Jun Woo KimNew Drug Development Center, Daegu-Gyeongbuk Medical Innovation Foundation, Daegu, South Korea.
Young-Jin SonNew Drug Development Center, Daegu-Gyeongbuk Medical Innovation Foundation, Daegu, South Korea.
Min Jung MaNew Drug Development Center, Daegu-Gyeongbuk Medical Innovation Foundation, Daegu, South Korea.
Jee-Hyun UmDepartment of Biochemistry, College of Medicine, Dong-A University, Busan, South Korea.
Nam Doo KimNew Drug Development Center, Daegu-Gyeongbuk Medical Innovation Foundation, Daegu, South Korea.
Sang Hyun MinNew Drug Development Center, Daegu-Gyeongbuk Medical Innovation Foundation, Daegu, South Korea.
Dong Il KimDepartment of Biological Engineering, Inha University, Incheon, South Korea.
Brian B KimR&D center, EncuraGen Inc, Anyang, Gyeonggi-do, South Korea.
Daegu-Gyeongbuk Medical Innovation Foundation · KRDong-A University · KRInha University · KRTheragen · KRYonsei University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Activation of adiponectin receptors (AdipoRs) by its natural ligand, adiponectin has been known to be involved in modulating critical metabolic processes such as glucose metabolism and fatty acid oxidation as demonstrated by a number of in vitro and in vivo studies over last two decades. These findings suggest that AdipoRs' agonists could be developed into a potential therapeutic agent for metabolic diseases, such as diabetes mellitus, especially for type II diabetes, a long-term metabolic disorder characterized by high blood sugar, insulin resistance, and relative lack of insulin. Because of limitations in production of biologically active adiponectin, adiponectin-mimetic AdipoRs' agonists have been suggested as alternative ways to expand the opportunity to develop anti-diabetic agents. Based on crystal structure of AdipoR1, we designed AdipoR1's peptide agonists using protein-peptide docking simulation and screened their receptor binding abilities and biological functions via surface plasmon resonance (SPR) and biological analysis. Three candidate peptides, BHD1028, BHD43, and BHD44 were selected and confirmed to activate AdipoR1-mediated signal pathways. In order to enhance the stability and solubility of peptide agonists, candidate peptides were PEGylated. PEGylated BHD1028 exhibited its biological activity at nano-molar concentration and could be a potential therapeutic agent for the treatment of diabetes. Also, SPR and virtual screening techniques utilized in this study may potentially be applied to other peptide-drug screening processes against membrane receptor proteins.

Indexed as

BiomimeticsAdiponectinBlood GlucoseDiabetes Mellitus, Type 2Fatty AcidsHumansInsulin ResistanceMolecular Docking SimulationOxidation-ReductionPeptidesProtein Interaction MapsReceptors, AdiponectinSignal TransductionSurface Plasmon ResonanceAdiponectinADIPOR1 protein, humanBlood GlucoseFatty AcidsPeptidesReceptors, Adiponectin

Identifiers

PMID29912982
PMCPMC6005460
OpenAlexW2808856645

What OpenQuestion holds

Textmetadata
LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.