Evidence map›Paper›PMID 26555191›Full record

ArticleFEBS letters2015

Role of arginine and lysine in the antimicrobial mechanism of histone-derived antimicrobial peptides.

Kara J Cutrona, Bethany A Kaufman, Dania M Figueroa, Donald E Elmore

Open access · bronzeAbstract read
In one paragraph

Article in FEBS letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

85 citing papers in PubMed, 196 citations in OpenAlex.

  1. Article
  2. From decay to discovery: A new antimicrobial peptide from Chrysomya megacephala (Diptera: Calliphoridae) larvae.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026
    Article
  3. Article
  4. Article
  5. Defining a lipophilicity window for the antimicrobial activity of 7-Alkoxy-3-Amino coumarin amphiphiles.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026
    Article
  6. Review
  7. Article
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  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Development of Low-Toxicity Antimicrobial Polycarbonates Bearing Lysine Residues.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024
    Article
  18. Article
  19. Article
  20. Review

25 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Kara J CutronaWellesley College, Department of Chemistry and Program in Biochemistry, 106 Central St., Wellesley, MA 02481, United States.
Bethany A KaufmanWellesley College, Department of Chemistry and Program in Biochemistry, 106 Central St., Wellesley, MA 02481, United States.
Dania M FigueroaWellesley College, Department of Chemistry and Program in Biochemistry, 106 Central St., Wellesley, MA 02481, United States.
Donald E ElmoreWellesley College, Department of Chemistry and Program in Biochemistry, 106 Central St., Wellesley, MA 02481, United States. Electronic address: delmore@wellesley.edu.
Wellesley College · US

Funding

Characterization and Design of Histone-Derived Antimicrobial PeptidesR15AI079685 · NIAID · WELLESLEY COLLEGE · PI ELMORE, DONALD E. · 2010 to 2015
$630k
NIAID NIH HHS R15 AI079685NIAID NIH HHS R15AI079685
6 · The paper itself

Abstract

Translocation of cell-penetrating peptides is often promoted by increased content of arginine or other guanidinium groups. However, relatively little research has considered the role of these functional groups on antimicrobial peptide activity. This study compared the activity of three histone-derived antimicrobial peptides-buforin II, DesHDAP1, and parasin-with variants that contain only lysine or arginine cationic residues. These peptides operate via different mechanisms as parasin causes membrane permeabilization while buforin II and DesHDAP1 translocate into bacteria. For all peptides, antibacterial activity increased with increased arginine content. Higher arginine content increased permeabilization for parasin while it improved translocation for buforin II and DesHDAP1. These observations provide insight into the relative importance of arginine and lysine in these antimicrobial peptides.

Indexed as

ArginineLysineAmino Acid SequenceAntimicrobial Cationic PeptidesCell MembraneHistonesMolecular Sequence DataMutationProtein TransportStructure-Activity RelationshipAntimicrobial Cationic PeptidesArginineHistonesLysineArginineBuforinHistone-derived antimicrobial peptideMembrane permeabilizationMembrane translocationParasin

Identifiers

PMID26555191
PMCPMC4713009
OpenAlexW2123231250

What OpenQuestion holds

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Read underepoch 390

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.