Evidence map›Paper›PMID 41098497›Full record

ArticleChemical science2025

Turn-engineering tunes the conformational rigidity of β-hairpin AMPs in achieving membrane selectivity and killing drug-resistant ESKAPE pathogens.

Priyanka Lahiri, Swati Priyadarshini, Mahak Saini, Muskan Agrawal, Sk Abdul Mohid, Raju S Rajmani, Vishnu S M Ammineni, Pritam Biswas, Aparna Asok, Amit K Baidya and 4 more

Abstract read
In one paragraph

Article in Chemical science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

14 authors.

Priyanka LahiriMolecular Biophysics Unit, Indian Institute of Science Bangalore India jayanta@iisc.ac.in.ORCID https://orcid.org/0000-0002-6971-1500
Swati PriyadarshiniMolecular Biophysics Unit, Indian Institute of Science Bangalore India jayanta@iisc.ac.in.ORCID https://orcid.org/0000-0002-3712-9620
Mahak SainiDepartment of Biosciences and Bioengineering, Indian Institute of Technology (Roorkee) Uttarakhand India.
Muskan AgrawalSolid State and Structural Chemistry Unit, Indian Institute of Science Bangalore India.
Sk Abdul MohidDepartment of Chemical Sciences, Bose Institute Unified Academic Campus Kolkata India.
Raju S RajmaniMolecular Biophysics Unit, Indian Institute of Science Bangalore India jayanta@iisc.ac.in.
Vishnu S M AmmineniMolecular Biophysics Unit, Indian Institute of Science Bangalore India jayanta@iisc.ac.in.
Pritam BiswasMolecular Biophysics Unit, Indian Institute of Science Bangalore India jayanta@iisc.ac.in.
Aparna AsokMolecular Biophysics Unit, Indian Institute of Science Bangalore India jayanta@iisc.ac.in.
Amit K BaidyaMolecular Biophysics Unit, Indian Institute of Science Bangalore India jayanta@iisc.ac.in.
Anirban BhuniaDepartment of Chemical Sciences, Bose Institute Unified Academic Campus Kolkata India.ORCID https://orcid.org/0000-0002-8752-2842
Govardhan ReddySolid State and Structural Chemistry Unit, Indian Institute of Science Bangalore India.ORCID https://orcid.org/0000-0002-9013-8040
Ranjana PathaniaDepartment of Biosciences and Bioengineering, Indian Institute of Technology (Roorkee) Uttarakhand India.ORCID https://orcid.org/0000-0002-7965-8176
Jayanta ChatterjeeMolecular Biophysics Unit, Indian Institute of Science Bangalore India jayanta@iisc.ac.in.ORCID https://orcid.org/0000-0002-4124-7339

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Naturally occurring β-hairpin antimicrobial peptides (AMPs) exhibit potent membranolytic activity against bacterial and mammalian cells, limiting their therapeutic development due to the lack of selectivity. This study demonstrates that the reverse turn in these AMPs can be used to dictate their molecular rigidity, which drives their membranolytic action. By fine-tuning the rigidity at the reverse turn by incorporating a moderately rigid β-II' turn-inducing motif through

Identifiers

PMID41098497
PMCPMC12520178

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