Evidence map›Paper›PMID 34055216›Full record

ArticleACS medicinal chemistry letters2021

De Novo Design, Synthesis, and Mechanistic Evaluation of Short Peptides That Mimic Heat Shock Protein 27 Activity.

Jessica Kho, P Chi Pham, Suhyeon Kwon, Alana Y Huang, Joel P Rivers, Huixin Wang, Heath Ecroyd, W Alexander Donald, Shelli R McAlpine

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS medicinal chemistry letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. Review
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

9 authors.

Jessica KhoSchool of Chemistry, University of New South Wales, Sydney, NSW 2052, Australia.
P Chi PhamSchool of Chemistry, University of New South Wales, Sydney, NSW 2052, Australia.
Suhyeon KwonSchool of Chemistry, University of New South Wales, Sydney, NSW 2052, Australia.
Alana Y HuangSchool of Chemistry, University of New South Wales, Sydney, NSW 2052, Australia.
Joel P RiversSchool of Chemistry, University of New South Wales, Sydney, NSW 2052, Australia.
Huixin WangSchool of Chemistry, University of New South Wales, Sydney, NSW 2052, Australia.
Heath EcroydDepartment of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, NSW 2522, Australia.ORCID 0000-0001-7574-0044
W Alexander DonaldSchool of Chemistry, University of New South Wales, Sydney, NSW 2052, Australia.ORCID 0000-0002-6622-8193
Shelli R McAlpineSchool of Chemistry, University of California Irvine, Irvine, California 92697, United States.ORCID 0000-0003-1058-5252

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We report the first small molecule peptides based on the N-terminal sequence of heat shock protein 27 (Hsp27, gene HSPB1) that demonstrates chaperone-like activity. The peptide, comprising the SWDPF sequence located at Hsp27's amino (N)-terminal domain, directly regulates protein aggregation events, maintaining the disaggregated state of the model protein, citrate synthase. While traditional inhibitors of protein aggregation act via regulation of a protein that facilitates aggregation or disaggregation, our molecules are the first small peptides between 5 and 8 amino acids in length that are based on the N-terminus of Hsp27 and directly control protein aggregation. The presented strategy showcases a new approach for developing small peptides that control protein aggregation in proteins with high aggregate levels, making them a useful approach in developing new drugs.

Identifiers

PMID34055216
PMCPMC8155270

What OpenQuestion holds

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Registered trials

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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.