ACS Applied Materials & Interfaces · 2019 · 81 citations · 46 references
Life SciencesBiochemistryBiotechnologyAntimicrobial ResistanceProtein FoldingStructural BiologyAntimicrobial PeptidesPeptide ChemistryProtein DesignProtein StructureProteolytic ProcessingResistance In Gram-negative BacteriaAntibacterial PeptidesAntimicrobial Peptide ActivityBactericidal AgentsCoiled-coil MotifsMembrane Disruption MechanismsPeptide Structure - Activity RelationshipsPeptide Structure-activity RelationshipsTherapeutic Peptides
= 294.25) with high stability toward salts, serum, extreme pH, heat, and proteases. Electron microscopy and biological analytical technique analyses showed that 3IH3 killed bacterial cells via a multicomplementary mechanism at pH 6.0, with physical membrane disruption as the dominant bactericidal mechanism. These results suggest that 3IH3 shows great stability as an inexpensive and effective antimicrobial activity agent and has the potential for clinical application in the treatment of infections occurring in body sites with acidic pH.
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