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

Toggling Preassembly with Single-Site Mutation Switches the Cytotoxic Mechanism of Cationic Amphipathic Peptides.

Journal of medicinal chemistry - 13 Feb 2020

Chen Xiaolong, Ji Shuangshuang, Li Ang, Liu Hanjie, Fei Hao

Abstract excerpt

Precise regulation of membrane-active peptide activity is a frontier of research to facilitate its applicational translation. A clear understanding of how a peptide's physicochemical properties determine its mode of action (MOA) will aid the process. Herein, anionic glutamate residue-based scanning was applied to the hydrophobic surface of a self-assembling lysine-rich cationic amphipathic peptide (CAP) KL1....

Read the complete abstract on PubMed

Topics

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

Share to Antineoplastic Agents
Share to Cell Membrane

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Erythrocytes

Share to Hemolysis

Share to Hydrophobic and Hydrophilic Interactions

Share to Peptides

Share to Protein Multimerization

Share to Surface-Active Agents

Source

Identifiers

PMID: 31927997
DOI: 10.1021/acs.jmedchem.9b01458

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

Toggling Preassembly with Single-Site Mutation Switches the Cytotoxic Mechanism of Cationic Amphipathic Peptides.PMID 31927997Read ↗

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 ↗

Improving the Antibacterial Activity of Tryptophan-Containing Peptide Nanostructures Through Self- AssemblySemantic proximity Read ↗

Extreme Hydrophobicity of Cytotoxic Drugs Enables Design of Next Generation Antibody-Drug Conjugates NanotherapeuticsSemantic proximity Read ↗

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

Anticancer Peptides: Design Principles, Translational Bottlenecks, and Emerging OpportunitiesSemantic proximity Read ↗

Intrinsically Selective Nanoplatforms for Precision Therapy and MonitoringSemantic proximity Read ↗

Effect of Leu/Val Mutation on the Energetics of Antimicrobial Peptide:Micelle Binding.Semantic proximity Read ↗

Iterative optimization yields Mcl-1-targeting stapled peptides with selective cytotoxicity to Mcl-1-dependent cancer cells.Semantic proximity Read ↗

Peptide Self-Assembly Is Linked to Antibacterial, but Not Antifungal, Activity of Histatin 5 Derivatives.Semantic proximity Read ↗

N-terminal amphipathic helix as a trigger of hemolytic activity in antimicrobial peptides: a case study in latarcins.Semantic proximity Read ↗

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

Switching Cytolytic Nanopores into Antimicrobial Fractal Ruptures by a Single Side Chain Mutation.Semantic proximity Read ↗

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