title: The proteome targets of intracellular targeting antimicrobial peptides.
abstract: Antimicrobial peptides have been considered well-deserving candidates to fight the battle against microorganisms due to their broad-spectrum antimicrobial activities. Several studies have suggested that membrane disruption is the basic mechanism of AMPs that leads to killing or inhibiting microorganisms. Also, AMPs have been reported to interact with macromolecules inside the microbial cells such as nucleic acids (DNA/RNA), protein synthesis, essential enzymes, membrane septum formation and cell wall synthesis. Proteins are associated with many intracellular mechanisms of cells, thus protein targets may be specifically involved in mechanisms of action of AMPs. AMPs like pyrrhocoricin, drosocin, apidecin and Bac 7 are documented to have protein targets, DnaK and GroEL. Moreover, the intracellular targeting AMPs are reported to influence more than one protein targets inside the cell, suggesting for the multiple modes of actions. This complex mechanism of intracellular targeting AMPs makes them more difficult for the development of resistance. Herein, we have summarized the current status of AMPs in terms of their mode of actions, entry to cytoplasm and inhibition of macromolecules. To reveal the mechanism of action, we have focused on AMPs with intracellular protein targets. We have also included the use of high-throughput proteome microarray to determine the unidentified AMP protein targets in this review.
authors.affiliation: Graduate Institute of Systems Biology and Bioinformatics, National Central University, Jhongli, Taiwan.|Department of Biomedical Science and Engineering, National Central University, Jhongli, Taiwan.
authors.forename: Pramod
authors.initials: P
authors.lastname: Shah
authors.affiliation: Graduate Institute of Systems Biology and Bioinformatics, National Central University, Jhongli, Taiwan.|Department of Biomedical Science and Engineering, National Central University, Jhongli, Taiwan.
authors.forename: Felix Shih-Hsiang
authors.initials: FS
authors.lastname: Hsiao
authors.affiliation: Graduate Institute of Systems Biology and Bioinformatics, National Central University, Jhongli, Taiwan.|Department of Biomedical Science and Engineering, National Central University, Jhongli, Taiwan.
authors.forename: Yu-Hsuan
authors.initials: YH
authors.lastname: Ho
authors.affiliation: Graduate Institute of Systems Biology and Bioinformatics, National Central University, Jhongli, Taiwan.|Department of Biomedical Science and Engineering, National Central University, Jhongli, Taiwan.
authors.forename: Chien-Sheng
authors.initials: CS
authors.lastname: Chen
mesh_terms: D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D042541:Intracellular Space / Q000378:metabolism*; D008826:Microbial Sensitivity Tests; D008954:Models, Biological; D020543:Proteome / Q000235:genetics / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*
chemical_list: D023181:Antimicrobial Cationic Peptides; D029968:Escherichia coli Proteins; D020543:Proteome
keywords: Antimicrobial peptides; Intracellular targets; Mechanism of action; Protein arrays; Protein targets; Proteome microarray