Evidence map›Paper›PMID 28054630›Full record

ArticleScientific reports2017

Disaggregation of Amylin Aggregate by Novel Conformationally Restricted Aminobenzoic Acid containing α/β and α/γ Hybrid Peptidomimetics.

Ashim Paul, Sourav Kalita, Sujan Kalita, Piruthivi Sukumar, Bhubaneswar Mandal

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

19 citing papers in PubMed, 42 citations in OpenAlex.

  1. QBP1 Peptide as a Potential Anti-Amyloidogenic Therapy for Type 2 Diabetes: An In Vitro Study.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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  13. The Role of Glycation on the Aggregation Properties of IAPP.Frontiers in molecular biosciences · 2020
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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

5 authors at 1 institution in 2 countries.

Ashim PaulLaboratory of Peptide and Amyloid Research, Department of Chemistry, Indian Institute of Technology Guwahati, Assam- 781039, India.
Sourav KalitaLaboratory of Peptide and Amyloid Research, Department of Chemistry, Indian Institute of Technology Guwahati, Assam- 781039, India.
Sujan KalitaLaboratory of Peptide and Amyloid Research, Department of Chemistry, Indian Institute of Technology Guwahati, Assam- 781039, India.
Piruthivi SukumarDepartment of Biosciences and Bioengineering, Indian Institute of Technology Guwahati, Assam-781039, India.
Bhubaneswar MandalLaboratory of Peptide and Amyloid Research, Department of Chemistry, Indian Institute of Technology Guwahati, Assam- 781039, India.
Indian Institute of Technology Guwahati · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Diabetes has emerged as a threat to the current world. More than ninety five per cent of all the diabetic population has type 2 diabetes mellitus (T2DM). Aggregates of Amylin hormone, which is co-secreted with insulin from the pancreatic β-cells, inhibit the activities of insulin and glucagon and cause T2DM. Importance of the conformationally restricted peptides for drug design against T2DM has been invigorated by recent FDA approval of Symlin, which is a large conformationally restricted peptide. However, Symlin still has some issues including solubility, oral bioavailability and cost of preparation. Herein, we introduced a novel strategy for conformationally restricted peptide design adopting a minimalistic approach for cost reduction. We have demonstrated efficient inhibition of amyloid formation of Amylin and its disruption by a novel class of conformationally restricted β-sheet breaker hybrid peptidomimetics (BSBHps). We have inserted β, γ and δ -aminobenzoic acid separately into an amyloidogenic peptide sequence, synthesized α/β, α/γ and α/δ hybrid peptidomimetics, respectively. Interestingly, we observed the aggregation inhibitory efficacy of α/β and α/γ BSBHps, but not of α/δ analogues. They also disrupt existing amyloids into non-toxic forms. Results may be useful for newer drug design against T2DM as well as other amyloidoses and understanding amyloidogenesis.

Indexed as

Protein AggregatesAminobenzoatesDiabetes Mellitus, Type 2HumansHypoglycemic AgentsIslet Amyloid PolypeptidePeptidomimeticsProtein Aggregation, PathologicalAminobenzoatesHypoglycemic AgentsIslet Amyloid PolypeptidePeptidomimeticsProtein Aggregates

Identifiers

PMID28054630
PMCPMC5214534
OpenAlexW2568863654

What OpenQuestion holds

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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.