Evidence map›Paper›PMID 34021253›Full record

ArticleCommunications biology2021

The lexicon of antimicrobial peptides: a complete set of arginine and tryptophan sequences.

Sam Clark, Thomas A Jowitt, Lynda K Harris, Christopher G Knight, Curtis B Dobson

Abstract read
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Artificial intelligence catalyzes antimicrobial peptide design.Synthetic and systems biotechnology · 2027
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Poly(ethylene Glycol)-Based Peptidomimetics (Pegtides) of Antimicrobial Peptides.Chembiochem : a European journal of chemical biology · 2025
    Article
  9. Article
  10. Deep-Learning Driven Identification of Novel Antimicrobial Peptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. PreventingACS applied materials & interfaces · 2024
    Article
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.

Sam ClarkDivision of Pharmacy & Optometry, School of Health Sciences, Stopford Building, The University of Manchester, Oxford Road, Manchester, UK.ORCID 0000-0002-6865-4452
Thomas A JowittWellcome Trust Centre for Cell-Matrix Research, The University of Manchester, Oxford Road, Manchester, UK.
Lynda K HarrisDivision of Pharmacy & Optometry, School of Health Sciences, Stopford Building, The University of Manchester, Oxford Road, Manchester, UK.
Christopher G KnightDepartment of Earth and Environmental Sciences, School of Natural Sciences, Michael Smith Building, The University of Manchester, Oxford Road, Manchester, UK.ORCID 0000-0001-9815-4267
Curtis B DobsonDivision of Pharmacy & Optometry, School of Health Sciences, Stopford Building, The University of Manchester, Oxford Road, Manchester, UK. curtis.dobson@manchester.ac.uk.ORCID 0000-0002-6483-4608

Funding

Biotechnology and Biological Sciences Research Council BB/M011208/1
6 · The paper itself

Abstract

Our understanding of the activity of cationic antimicrobial peptides (AMPs) has focused on well-characterized natural sequences, or limited sets of synthetic peptides designed de novo. We have undertaken a comprehensive investigation of the underlying primary structural features that give rise to the development of activity in AMPs. We consider a complete set of all possible peptides, up to 7 residues long, composed of positively charged arginine (R) and / or hydrophobic tryptophan (W), two features most commonly associated with activity. We found the shortest active peptides were 4 or 5 residues in length, and the overall landscapes of activity against gram-positive and gram-negative bacteria and a yeast were positively correlated. For all three organisms we found a single activity peak corresponding to sequences with around 40% R; the presence of adjacent W duplets and triplets also conferred greater activity. The mechanistic basis of these activities comprises a combination of lipid binding, particularly to negatively charged membranes, and additionally peptide aggregation, a mode of action previously uninvestigated for such peptides. The maximum specific antimicrobial activity appeared to occur in peptides of around 10 residues, suggesting 'diminishing returns' for developing larger peptides, when activity is considered per residue of peptide.

Indexed as

Amino Acid SequenceAnimalsAnti-Bacterial AgentsArginineBacteriaHemolysisHorsesPore Forming Cytotoxic ProteinsTryptophanAnti-Bacterial AgentsArgininePore Forming Cytotoxic ProteinsTryptophan

Identifiers

PMID34021253
PMCPMC8140080

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.