Effect of charge status on the ion transport and antimicrobial activity of synthetic channels

A class of unimolecular channels formed by pillararene-gramicidin hybrid molecules are presented. The charge status of the peptide domain in these channels has a significant impact on their ion transport and antimicrobial activity. These channels exhibited different membrane-association abilities be...

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Published inChemical communications (Cambridge, England) Vol. 56; no. 89; pp. 13796 - 13799
Main Authors Xin, Pengyang, Zhao, Lingyu, Mao, Linlin, Xu, Linqi, Hou, Shuaimin, Kong, Huiyuan, Fang, Haodong, Zhu, Haofeng, Jiang, Tao, Chen, Chang-Po
Format Journal Article
LanguageEnglish
Published England Royal Society of Chemistry 18.11.2020
Subjects
Animals
Anti-Bacterial Agents - chemistry
Anti-Bacterial Agents - pharmacology
Antibiotics
Antiinfectives and antibacterials
Antimicrobial agents
antimicrobial properties
Bacillus subtilis - drug effects
Calixarenes - chemistry
Calixarenes - pharmacology
Channels
Dose-Response Relationship, Drug
Erythrocytes - drug effects
Gramicidin - chemistry
Gramicidin - pharmacology
Ion Channels - antagonists & inhibitors
Ion Channels - metabolism
Ion transport
Ion Transport - drug effects
Ions
mammals
Microbial Sensitivity Tests
Microorganisms
Molecular Structure
NMR
Nuclear magnetic resonance
peptides
Rats
Staphylococcus aureus - drug effects
Toxicity
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Abstract A class of unimolecular channels formed by pillararene-gramicidin hybrid molecules are presented. The charge status of the peptide domain in these channels has a significant impact on their ion transport and antimicrobial activity. These channels exhibited different membrane-association abilities between microbial cells and mammalian cells. One of the channels displayed a higher antimicrobial activity towards S. aureus (IC 50 = 0.55 μM) and negligible hemolytic toxicity, showing potential to serve as a systemic antibiotic. The charge status of channels formed by pillararene-gramicidin hybrid molecules has a significant impact on their trans-membrane transport properties, membrane-association abilities and antimicrobial activities.
AbstractList A class of unimolecular channels formed by pillararene–gramicidin hybrid molecules are presented. The charge status of the peptide domain in these channels has a significant impact on their ion transport and antimicrobial activity. These channels exhibited different membrane-association abilities between microbial cells and mammalian cells. One of the channels displayed a higher antimicrobial activity towards S. aureus (IC50 = 0.55 μM) and negligible hemolytic toxicity, showing potential to serve as a systemic antibiotic.
A class of unimolecular channels formed by pillararene–gramicidin hybrid molecules are presented. The charge status of the peptide domain in these channels has a significant impact on their ion transport and antimicrobial activity. These channels exhibited different membrane-association abilities between microbial cells and mammalian cells. One of the channels displayed a higher antimicrobial activity towards S. aureus (IC 50 = 0.55 μM) and negligible hemolytic toxicity, showing potential to serve as a systemic antibiotic.
A class of unimolecular channels formed by pillararene–gramicidin hybrid molecules are presented. The charge status of the peptide domain in these channels has a significant impact on their ion transport and antimicrobial activity. These channels exhibited different membrane-association abilities between microbial cells and mammalian cells. One of the channels displayed a higher antimicrobial activity towards S. aureus (IC₅₀ = 0.55 μM) and negligible hemolytic toxicity, showing potential to serve as a systemic antibiotic.
A class of unimolecular channels formed by pillararene-gramicidin hybrid molecules are presented. The charge status of the peptide domain in these channels has a significant impact on their ion transport and antimicrobial activity. These channels exhibited different membrane-association abilities between microbial cells and mammalian cells. One of the channels displayed a higher antimicrobial activity towards S. aureus (IC 50 = 0.55 μM) and negligible hemolytic toxicity, showing potential to serve as a systemic antibiotic. The charge status of channels formed by pillararene-gramicidin hybrid molecules has a significant impact on their trans-membrane transport properties, membrane-association abilities and antimicrobial activities.
A class of unimolecular channels formed by pillararene-gramicidin hybrid molecules are presented. The charge status of the peptide domain in these channels has a significant impact on their ion transport and antimicrobial activity. These channels exhibited different membrane-association abilities between microbial cells and mammalian cells. One of the channels displayed a higher antimicrobial activity towards S. aureus (IC = 0.55 μM) and negligible hemolytic toxicity, showing potential to serve as a systemic antibiotic.
A class of unimolecular channels formed by pillararene-gramicidin hybrid molecules are presented. The charge status of the peptide domain in these channels has a significant impact on their ion transport and antimicrobial activity. These channels exhibited different membrane-association abilities between microbial cells and mammalian cells. One of the channels displayed a higher antimicrobial activity towards S. aureus (IC50 = 0.55 μM) and negligible hemolytic toxicity, showing potential to serve as a systemic antibiotic.A class of unimolecular channels formed by pillararene-gramicidin hybrid molecules are presented. The charge status of the peptide domain in these channels has a significant impact on their ion transport and antimicrobial activity. These channels exhibited different membrane-association abilities between microbial cells and mammalian cells. One of the channels displayed a higher antimicrobial activity towards S. aureus (IC50 = 0.55 μM) and negligible hemolytic toxicity, showing potential to serve as a systemic antibiotic.
Author Hou, Shuaimin
Chen, Chang-Po
Zhao, Lingyu
Xin, Pengyang
Xu, Linqi
Jiang, Tao
Zhu, Haofeng
Fang, Haodong
Mao, Linlin
Kong, Huiyuan
AuthorAffiliation Collaborative Innovation Center of Henan Province for Green Manufacturing of Fine Chemicals
Henan Normal University
Key Laboratory of Green Chemical Media and Reactions of Ministry of Education
School of Chemistry and Chemical Engineering
Henan Key Laboratory of Organic Functional Molecule and Drug Innovation
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– name: Key Laboratory of Green Chemical Media and Reactions of Ministry of Education
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– name: Henan Normal University
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/33078782$$D View this record in MEDLINE/PubMed
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  publication-title: Biophys. J.
  doi: 10.1016/S0006-3495(86)83642-6
SSID ssj0000158
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Snippet A class of unimolecular channels formed by pillararene-gramicidin hybrid molecules are presented. The charge status of the peptide domain in these channels has...
A class of unimolecular channels formed by pillararene–gramicidin hybrid molecules are presented. The charge status of the peptide domain in these channels has...
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SubjectTerms Animals
Anti-Bacterial Agents - chemistry
Anti-Bacterial Agents - pharmacology
Antibiotics
Antiinfectives and antibacterials
Antimicrobial agents
antimicrobial properties
Bacillus subtilis - drug effects
Calixarenes - chemistry
Calixarenes - pharmacology
Channels
Dose-Response Relationship, Drug
Erythrocytes - drug effects
Gramicidin - chemistry
Gramicidin - pharmacology
Ion Channels - antagonists & inhibitors
Ion Channels - metabolism
Ion transport
Ion Transport - drug effects
Ions
mammals
Microbial Sensitivity Tests
Microorganisms
Molecular Structure
NMR
Nuclear magnetic resonance
peptides
Rats
Staphylococcus aureus - drug effects
Toxicity
Title Effect of charge status on the ion transport and antimicrobial activity of synthetic channels
URI https://www.ncbi.nlm.nih.gov/pubmed/33078782
https://www.proquest.com/docview/2458974672
https://www.proquest.com/docview/2452508081
https://www.proquest.com/docview/2524311907
Volume 56
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linkProvider Royal Society of Chemistry
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