Journal of Agricultural and Food Chemistry · 2020 · 12 citations · 28 references
Life SciencesBiochemistryBiotechnologyProtein EngineeringStructural BiochemistryStructural BiologyAntimicrobial PeptidesPeptide ChemistryProtein ConformationProtein DesignProtein StructureAmphipathic Helical PeptidesAntibacterial PeptidesBactericidal AgentsBiological Activity FeaturesMutationPeptide Structure - Activity RelationshipsPeptide Structure-activity RelationshipsSynthetic Antimicrobial Peptide Design
-casein f (193-207) was modified by a defined mutation method to obtain five engineered peptides with mirror symmetry structures. The five engineered peptide sequences were WF-1 (WFQVKTRVRTKVQFW), FW-2 (FWRRYKKVKKYRRWF), FW-3 (FWQVIKKVKKIVQWF), FK-4 (FKQFYRRVRRYFQKF), and FR-5 (FRQWYRRVRRYWQRF). However, FW-2, FW-3, FK-4, and FR-5 had obvious XXYXX sequences. Among these, FW-3 was demonstrated to have the highest antibacterial activity, which indicates that the non-perfectly amphipathic α-helical structure containing the XXYXX sequence has a better bactericidal effect. Therefore, peptide FW-3 could be widely used as a substitute for antibiotics in food, medicine, and other fields. These findings provide a potential method for designing novel antimicrobial peptides.
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Optimization of the antimicrobial activity of magainin peptides by modification of charge
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Serum Stabilities of Short Tryptophan- and Arginine-Rich Antimicrobial Peptide Analogs
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