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Optimisation of Antimicrobial Peptide Design: Insights from Action Mechanisms Caleb M PostDoc Journal Journal of Postdoctoral Research Vol. 3, No. 6, June 2015 www.postdocjournal.com Optimisation of antimicrobial peptide design: insights from action mechanisms Caleb M. Agbale1,3, Osmel Fleitas 2,3, Isaac K. Galyuon1, Octavio L. Franco3,4 1 School of Biological Sciences, College of Agriculture and Natural Sciences, University of Cape Coast, Cape Coast, Ghana, 2 Pós-Graduação da Faculdade de Medicina. Campus Universitário Darcy Ribeiro, Universidade de Brasília, Asa Norte, Brasília, DF, Brasil, 3 S-Inova, Programa de Pós-Graduação em Biotecnologia, Universidade Católica Dom Bosco, 79117-900 Campo Grande, MS, Brasil, 4 Centro de Análises Proteômicas e Bioquímicas, Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia, Universidade Católica de Brasília, 70719-100 Brasília, DF, Brasil Email: [email protected] Abstract Antimicrobial peptides (AMPs) have emerged as one of several viable options for treatment of infections caused by multidrug-resistant microorganisms, which continue to pose the single greatest public health challenge to humankind. Unlike conventional antibiotics, AMPs affects several key extracellular and intracellular targets in bacteria simultaneously, drastically limiting chances of drug-resistance development. Over the years it has been possible to manipulate their chemical structures to design novel anti-infectives for the treatment of systemic and topical infections based on detailed information generated from structural-activity studies. These novel synthetic AMPs exhibit enhanced antimicrobial activity, less cytotoxicity to mammalian cells and enhanced stability to proteases. This review discusses some current developments that have expanded our understanding of their diverse killing mechanisms and shows how this has been employed in the design of AMPs with predictable activity. Introduction Detailed studies have outlined the series of molecular events by which AMPs induce cell AMPs are considered as natural antibiotics that death. Common themes identified are binding to play key functions in the innate immune system receptors on the cell surface, translocation of all living organisms. Unlike conventional across the cell membrane through pore antibiotics that inhibit a limited number of formation and accumulation of peptide, targets in microorganisms, AMPs attack a broad intracellularly followed by inhibition of critical range of extra- and intracellular targets biosynthetic pathways, protein synthesis and simultaneously, drastically limiting chances of DNA replication. Attempts will be made in the resistance development 1,2. Furthermore, several next section to discuss details of these AMPs including defensins and cathelicidns, mechanisms in the light of structural-activity display both immunomodulatory and relationships and how these have contributed to antimicrobial activities3,4. Currently, more than the design of more potent AMPs. 5,500 natural and synthetic AMPs with antimicrobial, antiviral, antiparasitic and The molecular dynamics of AMP-bacterial anticancer activities have been deposited in membrane interaction: the role of arginine, several peptide databases, including lysine and lipid composition http://aps.unmc.edu/AP/main.php/) and Dragon Antimicrobial Peptide Database (DAMPD, In spite of the large variability in their primary http://apps.sanbi.ac.za/dampd). Most of the structure, all cationic and anionic AMPs have the novel synthetic AMPs deposited in these ability to associate with anionic bacteria databases were designed using natural AMPs as membranes through long-range electrostatic templates5. interactions with the lipopolysaccharides or teichoic acids in the outer membrane of Gram- 15 Journal of Postdoctoral Research June 2015: 14–24 negative and Gram-positive bacteria, electrostatic interaction between Arg and Lys respectively. This interaction is facilitated by residues and LPS of Gram-negative bacteria or weak non-covalent bonds between the cationic teichoic acid of Gram-positive bacteria, because or anionic groups and phosphate groups in lipids, other amino acids such as Pro have been found nucleic acids and proteins, and hydroxyl or to modulate depth of insertion 17. It has been hydrogen of water. For anionic AMPs such as demonstrated that differences in the molecular dermicidin and maximinH5 this interaction with densities and constitution of the inner and outer the capsular polysaccharides is mediated by Zn leaflet of the membrane expressed as (2+) salt brides 6. The presence of a short site- spontaneous lipid curvature (SC) drastically specific H-bond distance of (~ 4 Å) between the influence the depth and orientation of insertion guanidinium-bearing carbon Cξ of Arg and (SC)18, 19. The SC influences the folding and ammonium-bearing carbon Cε of Lys and the insertion of α- helical and β-barrel AMPs into the phosphate of lipid head groups has been membranes. For example, α- helical AMPs adopt confirmed by solid state NMR, indicating the a parallel orientation in membranes with critical role of cationic amino acids in the negative SC such as 1-palmitoyl-2-oleoyl antimicrobial action of AMPs 7. The function of phosphatidylcholine (POPC), but assume a tilted the H-bond however, is not limited to the initial orientation or become completely buried in electrostatic attraction. Its formation enables the positive SC like dimyristoyl phosphatidylcholine peptide bond and charged residues to overcome (DMPC). For beta-barrel AMPs, a positive SC the Born repulsion and facilitates their insertion greatly facilitates membrane insertion, but into the lipid bilayer 8,9. This explains why insertion is severely limited in negative SC. abolishment or reduction of the hydrogen- These results highlight the interdependence of bonding ability in the guanidinium group either AMP insertion into membranes on peptide by dimethylation or charge reduction drastically backbone rigidity or flexibility, amphipathicity reduces antimicrobial activity in some AMPs, and lipid composition of the bacterial such as PG-110. Thus, the antimicrobial action of membrane. It is not possible to manipulate one AMPs is highly correlated with the Arg or Lys factor without affecting the others because they content, as confirmed by several studies using are not mutually exclusive. This explains why the histone-derived peptides – buforin II, role of primary structure in antimicrobial activity DesHDAP1, Arg-rich and Lys-rich histones11-13. must be considered on a one-on-one basis rather However, significant differences in the stabilities than a generalisation. of H-bond of Lys and Arg influence the depth of insertion into the bilipid layer and consequently AMPs that enter cells via membrane-bound 14 their contribution to antimicrobial activity . This surface receptors is because Lys –ammonium is monodentate and adopts a relatively mobile β-turn state in its The antimicrobial activity of several AMPs interaction with the phosphate head groups, appears to be dependent on interaction with resulting in the formation of a weak and membrane receptors as illustrated in Figure 120. transient H-bond. In contrast, Arg-guanidinium is These include lantibiotics such as copsin from bidentate and adopts a rigid β-strand Coprinopsis cinerea21,22, the fungal defensin, conformation which stabilises the H-bond and eurocin from Eurotium amstelodami 23, human favours a deeper insertion into bacterial cell AMPs such as HNP-1 and hBD-324 and teixobactin membrane. The difference in stability of H-bonds from Eleftheria terrae 25, which bind to lipid II on explains the several observations of changes in the bacterial surface. Lipid is required in shuttling antimicrobial activity in Lys- for- Arg of building blocks for peptidoglycan synthesis, substitution15,16. It must be stated emphatically and disruption of its activity severely impairs cell that depth of insertion into membranes is wall synthesis. Overall, it appears that blocking of multifaceted and not dependent only on bacterial cell wall synthesis via lipid II binding is a Abgal C.M. et al. 16 common but very potent antimicrobial strategy AMP1 from Dahlia merckii has been found to among all eukaryotes and prokaryotes, possibly exhibit its fungicidal activity in S. cerevisiae using due to its highly conserved domain25, and this M(IP)2C as a receptor. This is premised on the represents an attractive target for drug observation that S. cerevisiae strains with a non- development. functional IPT1 allele, the gene that codes for M(IP)2C receptors, and thus lacking M(IP)2C in Recently, several receptors other than lipid II their membranes, were found to be highly have been described in bacteria. These include resistant towards DmAMP1 as compared to the UppP (undecapreny pyrophophosphate wild type (WT)31. Some antifungal proteins such phosphatase), the enzyme involved in the as Penicillium chrysogenum antifungal protein biosynthesis of lipopolysaccharide and (PAF) have been reported to act through a G- peptidoglycan, which acts as a receptor for protein-coupled signal transduction pathway, lactococcin G and enterocin 1071 (two-chain triggering cell death by apoptosis or inducing 26 bacteriocins) . Garvicin ML (GarML) and the imbalance in Ca(+2) homeostasis in filamentous leaderless class II bacteriocin LsbB, produced by fungi, including Aspergillus nidulans and Lactococcus lactis subsp. lactis BGMN1- Aspergillus fumigatus 32. 5,interact with receptors such as maltose ABC transporter and the yvjB gene, respectively 27,28. The maltose ABC transporter plays a critical role in starch
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