Evidence map›Paper›PMID 34263169›Full record

ReviewRSC medicinal chemistry2021

Cyclisation strategies for stabilising peptides with irregular conformations.

Quynh Ngoc Vu, Reginald Young, Haritha Krishna Sudhakar, Tianyi Gao, Tiancheng Huang, Yaw Sing Tan, Yu Heng Lau

Abstract readReview
In one paragraph

Review in RSC medicinal chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

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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

7 authors.

Quynh Ngoc VuSchool of Chemistry, Eastern Ave, The University of Sydney NSW 2006 Australia yuheng.lau@sydney.edu.au.
Reginald YoungSchool of Chemistry, Eastern Ave, The University of Sydney NSW 2006 Australia yuheng.lau@sydney.edu.au.
Haritha Krishna SudhakarSchool of Chemistry, Eastern Ave, The University of Sydney NSW 2006 Australia yuheng.lau@sydney.edu.au.
Tianyi GaoSchool of Chemistry, Eastern Ave, The University of Sydney NSW 2006 Australia yuheng.lau@sydney.edu.au.
Tiancheng HuangSchool of Chemistry, Eastern Ave, The University of Sydney NSW 2006 Australia yuheng.lau@sydney.edu.au.ORCID https://orcid.org/0000-0002-0993-3742
Yaw Sing TanBioinformatics Institute, Agency for Science, Technology and Research (ASTAR) 30 Biopolis Street, #07-01, Matrix Singapore 138671 Singapore.ORCID https://orcid.org/0000-0002-2522-9421
Yu Heng LauSchool of Chemistry, Eastern Ave, The University of Sydney NSW 2006 Australia yuheng.lau@sydney.edu.au.ORCID https://orcid.org/0000-0001-6560-8410

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclisation is a common synthetic strategy for enhancing the therapeutic potential of peptide-based molecules. While there are extensive studies on peptide cyclisation for reinforcing regular secondary structures such as α-helices and β-sheets, there are remarkably few reports of cyclising peptides which adopt irregular conformations in their bioactive target-bound state. In this review, we highlight examples where cyclisation techniques have been successful in stabilising irregular conformations, then discuss how the design of cyclic constraints for irregularly structured peptides can be informed by existing β-strand stabilisation approaches, new computational design techniques, and structural principles extracted from cyclic peptide library screening hits. Through this analysis, we demonstrate how existing peptide cyclisation techniques can be adapted to address the synthetic design challenge of stabilising irregularly structured binding motifs.

Identifiers

PMID34263169
PMCPMC8230030

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.