Publication | Closed Access
A unimolecular channel formed by dual helical peptide modified pillar[5]arene: correlating transmembrane transport properties with antimicrobial activity and haemolytic toxicity
22
Citations
48
References
2017
Year
Proteinlipid InteractionPeptide EngineeringTransmembrane Transport PropertiesSystemic AntibioticsAntimicrobial ChemotherapyUnimolecular ChannelsDrug ResistanceMembrane TransportUnimolecular ChannelAntimicrobial ResistanceBiochemistryAntibacterial AgentMembrane SystemProtein TransportAntimicrobial CompoundPharmacologyClinical MicrobiologyDual Helical PeptideBiomolecular EngineeringAntimicrobial SusceptibilityAntibioticsNatural SciencesProtein EngineeringAntimicrobial ActivityMicrobiologyMedicine
Five unimolecular channels with different lengths are presented. The varying length of these channels has significant impact on their transmembrane transport properties, which are directly correlated with their antimicrobial activity and inversely correlated with their haemolytic toxicity. By further structural optimization, these new channels could reach high antimicrobial activity and very low haemolytic toxicity, with the potential to serve as systemic antibiotics.
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