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

Molecular design of antimicrobial peptides based on hemagglutinin fusion domain to combat antibiotic resistance in bacterial infection.

Journal of peptide science : an official publication of the European Peptide Society - 1 Mar 2018

Ye Hui

Abstract excerpt

Antimicrobial peptides are derived from the viral fusion domain of influenza virus hemagglutinin based on rational analysis of the intermolecular interaction between peptides and bacterial outer membrane. It is revealed that the isolated viral fusion domain is a negatively charged peptide HAfp1-23 that cannot effectively interact with the anionic membrane. Conversion of the native HAfp1-23 to a positively charged...

Read the complete abstract on PubMed

Topics

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

Share to Antimicrobial Cationic Peptides
Share to Cyclization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drug Resistance, Multiple, Bacterial

Share to Entropy

Share to Hemagglutinins, Viral

Share to Methicillin-Resistant Staphylococcus aureus

Share to Orthomyxoviridae

Share to Pseudomonas aeruginosa

Source

Identifiers

PMID: 29542264
DOI: 10.1002/psc.3068

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

Molecular design of antimicrobial peptides based on hemagglutinin fusion domain to combat antibiotic resistance in bacterial infection.PMID 29542264Read ↗

Improving Conformational Stability and Bacterial Membrane Interactions of Antimicrobial Peptides with Amphipathic Helical StructureSemantic proximity Read ↗

Role of amphipathicity and hydrophobicity in the balance between hemolysis and peptide-membrane interactions of three related antimicrobial peptides.Semantic proximity Read ↗

Development of novel broad-spectrum amphipathic antimicrobial peptides against multidrug-resistant bacteria through a rational combination strategySemantic proximity Read ↗

Innovative Strategies and Methodologies in Antimicrobial Peptide DesignSemantic proximity Read ↗

Potent peptidic fusion inhibitors of influenza virusSemantic proximity Read ↗

Adapting antibacterial display to identify serum active macrocyclic peptide antibioticsSemantic proximity Read ↗

Effective antimicrobial activity of a peptide mutant Cbf-14-2 against penicillin-resistant bacteria based on its unnatural amino acids.Semantic proximity Read ↗

Local structural constraints and charge distribution in the protegrin-1 arginine loop govern activity against colistin-resistant Klebsiella pneumoniae.Semantic proximity Read ↗

Nonhemolytic Cell-Penetrating Peptides: Site Specific Introduction of Glutamine and Lysine Residues into the α-Helical Peptide Causes Deletion of Its Direct Membrane Disrupting Ability but Retention of Its Cell Penetrating Ability.Semantic proximity Read ↗

Hybrid Derivative of Cathelicidin and Human Beta Defensin-2 Against Gram-Positive Bacteria: A Novel Approach for the Treatment of Bacterial KeratitisSemantic proximity Read ↗

Decoding the functional roles of cationic side chains of the major antimicrobial region of human cathelicidin LL-37.Semantic proximity Read ↗

Investigation of the mutated antimicrobial peptides to inhibit ACE2, TMPRSS2 and GRP78 receptors of SARS-CoV-2 and angiotensin II type 1 receptor (AT1R) as well as controlling COVID-19 disease.Semantic proximity Read ↗

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