Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

FEBS letters - 21 Dec 2015

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

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Antimicrobial Cationic Peptides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Arginine

Share to Cell Membrane

Share to Histones

Share to Lysine

Share to Protein Transport

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 26555191
DOI: 10.1016/j.febslet.2015.11.002
PMCID: PMC4713009

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of arginine and lysine in the antimicrobial mechanism of histone-derived antimicrobial peptides.PMID 26555191Read ↗

Antibacterial PeptidesSemantic proximity Read ↗

D-amino acid substitution and cyclisation enhance the stability and antimicrobial activity of arginine-rich peptidesSemantic proximity Read ↗

Cationic antimicrobial peptide resistance mechanisms of streptococcal pathogensSemantic proximity Read ↗

Antimicrobial and anti-inflammatory activities of three chensinin-1 peptides containing mutation of glycine and histidine residues.Semantic proximity Read ↗

Multiple peptide resistance factor (MprF)-mediated Resistance of Staphylococcus aureus against antimicrobial peptides coincides with a modulated peptide interaction with artificial membranes comprising lysyl-phosphatidylglycerol.Semantic proximity Read ↗

The antimicrobial potentialities of (Nk-lysin peptides of chicken, bovine, and human) against bacteria and rotavirusSemantic proximity Read ↗

Antimicrobial peptides of multicellular organisms.Semantic proximity Read ↗

Antimicrobial activity of cationic antimicrobial peptides against stationary phase bacteriaSemantic proximity Read ↗

Identification of novel Amurin-2 variants from the skin secretion of Rana amurensis, and the design of cationicity-enhanced analogues.Semantic proximity Read ↗

Antimicrobial activity of the recombinant peptide Melittin-Thanatin with three glycine to tryptophan mutations.Semantic proximity Read ↗

Surface-exposed amino acids of eosinophil cationic protein play a critical role in the inhibition of mammalian cell proliferation.Semantic proximity Read ↗

Inhibition of Furin by Polyarginine-containing PeptidesSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.