Guide Antimicrobial Peptides (Advances in Molecular and Cellular Biology Series)

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Changing these features will help to modify the activity and target spectrum of AMPs. The length of an AMP is important to its activity because at least 7—8 amino acids are needed to form amphipathic structures with hydrophobic and hydrophilic faces on opposite sides of a peptide molecule. Besides the effects of length on its 3D structure and mode of action, the length of an AMP may also affect its cytotoxicity. For example, a shortened melittin with 15 residues at its C-terminal [ ] and a shorter derivative of HP [ ] exhibited at least times less toxicity to rat erythrocytes and human erythrocytes, respectively, compared to their original forms.

Therefore the length of AMP should be taken into consideration when designing new synthetic peptides with low toxicity. The net charge of known AMPs, which is the sum of all charges of ionizable groups of the peptide, varies from negative to positive and it is the main factor for the initial interaction with negatively charged cell membranes.

By changing the net charge of an AMP, its antimicrobial and hemolytic activities can be altered to achieve selective killing of microbes with no or minimized effects on host cells. Helicity represents the ability of an AMP to form spin structure. It is less important for the activity of an AMP compared to other factors discussed above. However, it is important for determining the toxicity on eukaryotic cells [ 6 ]. Reducing helicity by incorporating d -amino acids into the primary sequence has been shown to lower the hemolytic effect, while the antimicrobial effect was retained [ ].


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For example, Papo et al. Besides, these new synthetic AMPs are not sensitive to proteases. Therefore, incorporating d -amino acids to change helicity is a useful strategy for designing new synthetic peptides with less hemolytic activity and enhanced stability against proteolytic cleavage. Another important factor associated with the helicity of AMP is the helix propensity of each amino acid in the primary sequence. For example, proline and glycine have lower helix-forming propensities compared to other amino acids [ ].

In addition, peptides should be flexible enough to change their conformation during the membrane insertion process [ 47 ]. Hydrophobicity has also been shown to influence the activity and selectivity of AMP molecules. In most cases, increase in hydrophobicity on the positively charged side of an AMP below a threshold can increase its antimicrobial activity [ 6 ], while decreasing hydrophobicity can reduce antimicrobial activity [ ]. There appears to be an optimal hydrophobicity for each AMP, beyond which its activity decreases rapidly [ ]. Therefore, when designing new synthetic peptides, the hydrophobicity should be selected within an optimal window.

Some previous studies have shown that hydrophobicity is also critical for determining the range of target cells of an AMP. Increasing the hydrophobicity of an AMP can change the range of targets [ , ]. For example, magainin is an AMP that is only effective against Gram-negative bacteria. However, some synthetic analogs with higher hydrophobicity can also kill some Gram-positive bacteria and eukaryotic cells [ ].

Amphipathicity is another important property of AMPs to ensure their activity and interaction with microbial membranes. Fernandes-Vidal et al. Because amphipathicity of AMPs is required for a strong partition into the membrane interface, priority should be given to the amphipathic structure when designing synthetic AMPs for specific target cells.

Since AMPs should act on or enter through lipid membranes, they need to be soluble in aqueous environments. If AMP molecules aggregate, it will lose its ability to interact with the cell membrane. For example, a hybrid synthetic AMP composed of cecropin and melittin has a tendency to form dimers. Substituting a Lys residue on the non-polar face of this hybrid AMP prevents dimerization and leads to reduced hemolytic activity. Losing dimerization ability makes this AMP more effective for its incorporation into microbial membranes [ ]. This example demonstrates the importance of solubility and the value of structural optimization.

As discussed above, many factors affect the activities of AMPs and some interactions exist between these factors. In AMP design, these properties need to be considered together since changing one of these parameters to get a desired modification of an AMP may alter other parameters.

Even a simple change in primary sequence can affect many other physicochemical parameters which are often vital for the activity of an AMP and the range of target cells [ ]. Predicting the results of an AMP modification or the function of a synthetic peptide beforehand is still an unmet challenge. Application of molecular simulation to analyze the details of the folding of AMP molecules and interaction with target cells [ , ] may be a promising approach to improve current trial and error methods.

While most of AMPs are directly synthesized in their active forms, post-translational modification of certain AMPs is necessary for their functions. Naturally forming AMPs are processed with different post-translational modifications such as phosphorylation [ ], addition of d -amino acids [ , ], methylation [ ], amidation [ ], glycosylation [ ], formation of disulphide linkage [ ], and proteolytic cleavage [ 24 , ]. In some cases, these posttranslational modifications might be important for designing new synthetic AMPs. Even though recombinant cell systems can be used to produce these synthetic peptides with post-translational modifications, incorporation of unnatural amino acids may require chemical synthesis [ 60 ].

Covalent modification can have profound effects on the structure and function of an AMP. Even a single disulfide bond can change the antimicrobial effect of an AMP. For example, protegrin missing a disulphide bond becomes inactive against HSV [ ]; while adding disulphide bond in sakacin P resulted in higher antimicrobial activities [ 44 ].

In another study, a disulfide bond was added in CP, a derivative of indolicidin [ ], and a trp-trp cross-link was added in indolicin [ ]. These modified structures of indolicidins showed higher protease stability with no change in antimicrobial activity. However increase in stability does not always lead to better AMPs. For example, Houston et al. Alteration of amino acid content is one of the most studied strategies of AMP modification. Most of these studies focus on certain amino acids since their physiological characteristics play important roles in the activity and target spectrum of AMPs.

For example proline content in the primary sequence of an AMP has been found to affect its ability to penetrate cell membranes. Higher proline content reduces the capability of CP26 to permeablize E. Changing amino acid content can also affect cytotoxicity. In a study by Nell et al. The new synthetic peptide showed less cytotoxic effects on eukaryotic cells. This peptide was named P Another strategy to improve AMP stability is to include, d -amino acids in the sequence because they are more tolerant to proteases [ , ]. With new developments in peptide synthesis, it is possible to incorporate special chemical groups or unnatural molecules into AMPs.

One of these modifications is the addition of amide groups at the end of the peptides. In , Kim et al. This modification resulted in almost 10 fold higher cellular uptake, faster interaction with Gram-negative bacteria cell membrane, and deeper insertion into the inner membrane than the original PMAP This carboxyl-end amidated synthetic peptide also showed better membrane-permeabilization in liposome release tests [ ]. Therefore amidation of carboxyl end has good potential to improve the function of synthetic AMPs. C-terminal modifications can also affect the stability of AMPs. In a previous study by Berthold et al.

This modification did not change its antimicrobial activity, but resulted in a 15 times more stable Api88 derivative against proteases in blood serum. Replacing Arg of this AMP with l -ornithine or l -homoarginine gave 35 times higher proteolytic stability than the original Api However, the latter modification decreased the antimicrobial activity by eight fold [ ]. A number of studies on synthetic peptides have attempted to incorporate unnatural amino acids into the primary sequence [ 99 , , ].

It is widely used in medicinal chemistry to alter the native bioactive AMPs [ ]. Researchers have also been able to introduce antifungal activities to some AMPs by incorporating undecanoic acid and palmitic acid into their primary sequence [ 99 , ]. The use of computer-assisted methods in AMP research has been increasing significantly [ , , , , , ]. Estimating the structure of an AMP based on its primary sequence [ ], then predicting potential mechanism of action and activity is becoming easier with the help of computational approaches [ ].

These types of artificial AMP design strategies hold potential for developing new synthetic peptides against antibiotic-resistant superbugs [ ]. For example, Tossi et al. These natural AMPs are composed mainly of cecropins, magainins, brevinins, and cathelicidin peptides sourced from insects, amphibian, and mammals. This synthetic peptide study focused on the first 20 amino acids in each sequence because the N-terminal region was shown to be necessary for antimicrobial activities [ , ]. These synthetic AMPs exhibited antimicrobial activities against Gram-positive and Gram-negative bacteria, including some drug resistant strains.

In addition, these synthetic AMPs showed low toxicity to some eukaryotic cell lines [ ]. Designing synthetic AMPs by homology modeling within the same class might also provide a better understanding of activity-structure relationship. Important elements from the same AMP class may be identified using this approach to help design better molecules.

Storici et al. This short synthetic peptide was found to induce permeabilization of the inner membrane of E. These new synthetic AMPs showed lower cytotoxicity compared to the original AMPs and exhibited dose dependent antimicrobial activities 0. It is also possible to broaden the target spectrum of an AMP by homology modeling. For example, normally lactoferrampins are not effective against E. This common region was modified by inserting GKLI sequence into its primary sequence, and the new synthetic peptide showed activities against E.

Because AMPs can directly target bacterial cells, they have potential to control antibiotic tolerant cells. Here we review some recent work on biofilms and persister cells. Biofilms are immobile bacterial populations attached to surfaces such as human tissues and medical implants. With cells protected by an extracellular matrix, biofilms are highly tolerant to antimicrobials [ ] and are a major cause of chronic infections; e.

In addition to the protection by the extracellular matrix [ ], biofilm associated antibiotic resistance is also attributed to the slow growth of biofilm cells [ ]. Even though some antibiotics have been shown to effectively penetrate biofilm matrix [ ], they are not effective against these slowly growing cells, especially the dormant subpopulation known as persister cells [ , , ]. Since most AMPs target cell membrane, they may be more effective against these dormant cells compared to antibiotics.

The first obstacle of using AMPs against biofilms is the possible electrostatic interaction between cationic peptides and negatively charged biofilm matrix [ ]. Such interactions may retard or prevent AMPs from reaching biofilm cells. Previous studies have investigated the effects of some AMPs on biofilm inhibition and killing of bacterial cells in established biofilms.

The second type of study is especially important since treatment of mature biofilms is highly challenging [ ]. In a study by Singh et al. This AMP also showed activity against preformed 2-days old P. In another study, a derivative of LL was found effective against both Gram-positive and Gram-negative bacteria.

Despite its weak antimicrobial activity against planktonic cells, this AMP inhibited biofilm formation of P. The same study showed that this inhibition is due to decrease in swarming and swimming motilities, increase in twitching motility, and repression of some biofilm genes. In addition to free AMPs, surface coating with AMPs has also been pursued since surface modifications with AMPs might help reduce device associated infections [ , , , ]. Many AMPs have been tested for their inhibitory effects on biofilm formation on implant surfaces. It is able to stop biofilm formation and appears to be non-toxic to eukaryotic cells [ ].

The conjugates of both AMPs resulted in higher binding efficiency to Ti surfaces than AMPs alone and Porphyromonas gingivalis showed less ATP activity and reduced biofilm formation on coated surfaces [ ]. A synthetic histatin analogue dhvar4 was tested against oral flora on hydroxyapatite disks and this AMP reduced the number of viable biofilm cells by 1.

However, it also led to some toxicity and proinflammation in the sinuses [ ]. As discussed above, the extracellular matrix of a biofilm is thought to form a diffusion barrier against certain AMPs [ ]. It is known that this negatively charged barrier protects the cells inside from positively charged antimicrobial agents and the alginate in biofilm matrix can reduce the diffusion of antimicrobial agents [ ].

Thus, it is important to obtain AMPs that can diffuse into biofilms and kill biofilm cells. Recently a synthetic peptide, RW 4D dendrimer [ ] was demonstrated to inhibit planktonic growth and biofilm formation of E.


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  7. This AMP inhibited biofilm formation by This dendrimer did not detach preformed biofilms, but was able to kill most of the cells residing in mature biofilms dose dependently [ ]. The chain length was found to be important to the activity of these peptides. This length-activity relation was also found for biofilm inhibition. Preformed biofilms were also tested with these peptides. However, the treatment of preformed biofilms with these peptides did not show the same length-activity relationship. AMPs have also been tested against the biofilms of drug resistant bacteria. In a study by Okuda et al.

    NRC, a synthetic peptide, was tested against biofilm formation of three P. There are also some AMPs that can sensitize biofilm cells to other antimicrobial agents. For example, lactoferrin does not kill S. However treatment of S. Persisters cells can be found in almost any microbial populations. These cells are dormant phenotypic variants and are highly tolerant to antibiotics [ ].

    However, membrane integrity is essential for the survival of bacteria irrespective of the metabolic stage of the cell and cell membrane is a major target of AMPs. Thus, AMPs may have good potential to kill persister cells. Thus, the combination of conventional antibiotics with AMPs may offer a synergy to control drug tolerant infections. There are mainly two different types of resistance mechanisms against AMPs: constitutive resistance and inducible resistance [ ]. The inducible resistance mechanisms include substitution [ ], modification [ ], and acylation [ ] of the membrane molecules, activation of some proteolytic enzymes [ ] and efflux pumps [ ], and modifications of intracellular targets [ ].

    The constitutive resistance mechanisms include electrostatic shielding [ ], changes in membrane potential during different stages of cell growth [ ], and biofilm formation [ ]. These resistance mechanisms are illustrated in Figure 3. Schematic representation of AMP resistance mechanisms. C Bacteria express some positively charged proteins and integrate them in the membrane so positive charges repulse each other and bacteria can resist such AMPs. D Bacteria produce negatively charged proteins and secrete them into extracellular environment to bind and block AMPs.

    E The intracellular AMPs are extruded by efflux pumps. F The AMPs inside the cell are degraded by proteases. For example the activity of some AMPs against S. These adhesin molecules are polymeric substances and stay on the cell surface after secretion [ ]. Since adhesin is a positively charged polymer, it can form a repulsive barrier against positively charged AMPs. Salmonella typhimurium also has a membrane bound lipid A modification system, which defends themselves against AMPs from the host [ ]. In this system, PhoQ is a membrane bound sensor kinase and PhoP is intracellular response regulator.

    PhoQ is activated in the presence of high level positive charges outside the cells. It then phosphorylates the PhoP causing up-regulation of some genes including those related to AMP resistance. Although bacteria have diverse mechanisms for resistance to AMPs, it is encouraging to notice that the general lipid bilayer structure of bacterial membranes makes it hard to develop a complete resistance against AMPs. Also, the resistance against AMPs reported to date is not as strong as those against antibiotics and it only covers a limited number of AMPs. The urgent need to obtain new antimicrobials has been driving AMP research.

    With rapid growth in related knowledge and lead compounds, more AMPs may enter clinical tests and treatment in the near feature. However, infection control by AMP is still hindered by several challenges including low specificity, high manufacturer cost, potential toxicity to animal cells, and lack of a robust guideline for rational design. As we have seen from synthetic and modified AMP studies, it is easy to change characteristics of an AMP with even small modifications.

    However, predicting the results of these changes is still challenging. Thus, there is a need to understand the effects of structural modifications on the physiochemical characteristics of AMPs as well as their target spectrum and activity. Recently, these types of studies have been increasing and computational approaches have been involved in AMP research. These efforts will help to better understand the mode of action of AMPs and predict their activities.

    Another understudied area is using AMPs to control antibiotic resistant bacteria, biofilms, and persisters. These targets are highly resistant to traditional antibiotics and play important roles in infections. Since AMPs target cell membrane, they have good potential in such applications. On the other hand, because AMPs have not been well studied for biofilm and persister control, there might be some existing natural AMPs that are effective against these targets with potential synergy with antibiotics.

    Applying AMPs with biofilm matrix degrading enzymes might also be a good strategy to eliminate biofilms. Further development in this area and AMP research in general will benefit from close collaboration of different disciplines and new tools that can decipher the structure-function relationship and more efficiently synthesize and modify AMP molecules. National Center for Biotechnology Information , U. Journal List Pharmaceuticals Basel v. Pharmaceuticals Basel. Published online Nov Author information Article notes Copyright and License information Disclaimer.

    This article has been cited by other articles in PMC. Abstract The rapid increase in drug-resistant infections has presented a serious challenge to antimicrobial therapies. Keywords: antimicrobial peptide, biofilm, persister. Sources and History of Antimicrobial Peptides Antimicrobial peptides AMPs are oligopeptides with a varying number from five to over a hundred of amino acids. Open in a separate window. Figure 1. Classification In general, enzymatic mechanisms are not involved in the antimicrobial activities of AMPs [ 65 ].

    Antiviral Peptides Antiviral AMPs neutralize viruses by integrating in either the viral envelope or the host cell membrane. Antibacterial Peptides Antibacterial AMPs are the most studied AMPs to date and most of them are cationic AMPs, which target bacterial cell membranes and cause disintegration of the lipid bilayer structure [ 81 , 82 ]. Antifungal Peptides Like antibacterial AMPs, antifungal peptides can kill fungi by targeting either the cell wall [ 88 , 89 ] or intracellular components [ 90 ].

    Antiparasitic Peptides Antiparasitic peptides are a smaller group compared to other three AMP classes. Mechanism of Action As described above, AMPs kill cells by disrupting membrane integrity via interaction with negatively charged cell membrane , by inhibiting proteins, DNA and RNA synthesis, or by interacting with certain intracellular targets. Membrane-Active AMPs Even if intracellular targets are involved, an initial cell membrane interaction with peptides is required for the antimicrobial activities of AMPs [ ]; and this interaction determines the spectrum of target cells.

    Table 1 The action mechanisms of membrane-active AMPs. Interaction model Mechanism References Carpet like Detergent-like The peptide micelle touches the membrane first and coats a small area of the membrane. Then AMP molecules penetrate the lipid bilayer to let pore formation occur leaving holes behind. It can form a gap between lipid molecules at the chain region. This gap creates a force and pulls the neighboring lipid molecules to fill it. Then reorientation of AMPs occurs and they insert themselves into the membrane vertically to form sphere-like structures.

    Then barrels are formed and AMPs are inserted perpendicularly to the plane of the membrane bilayer. Figure 2. Designing New Synthetic AMPs: Major Factors to Consider To date, no data have been reported to demonstrate a clear relationship between the structural groups of an AMP and its mode of action, the degree of activity, or the host range.

    Length The length of an AMP is important to its activity because at least 7—8 amino acids are needed to form amphipathic structures with hydrophobic and hydrophilic faces on opposite sides of a peptide molecule. Net Charge The net charge of known AMPs, which is the sum of all charges of ionizable groups of the peptide, varies from negative to positive and it is the main factor for the initial interaction with negatively charged cell membranes. Helicity Helicity represents the ability of an AMP to form spin structure. Hydrophobicity Hydrophobicity has also been shown to influence the activity and selectivity of AMP molecules.

    Amphipathicity Amphipathicity is another important property of AMPs to ensure their activity and interaction with microbial membranes. Solubility Since AMPs should act on or enter through lipid membranes, they need to be soluble in aqueous environments. Modification of AMPs by Amidation With new developments in peptide synthesis, it is possible to incorporate special chemical groups or unnatural molecules into AMPs. Modification of AMPs with Unnatural Amino Acids A number of studies on synthetic peptides have attempted to incorporate unnatural amino acids into the primary sequence [ 99 , , ].

    Biofilm Control The first obstacle of using AMPs against biofilms is the possible electrostatic interaction between cationic peptides and negatively charged biofilm matrix [ ]. Persister Control Persisters cells can be found in almost any microbial populations. Resistance to Antimicrobial Peptides There are mainly two different types of resistance mechanisms against AMPs: constitutive resistance and inducible resistance [ ]. Figure 3. Conclusions The urgent need to obtain new antimicrobials has been driving AMP research. Conflicts of Interest The authors declare no conflict of interest.

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    Japanese Journal of Cancer Research, , vol. TANG, Y. It seems that you're in Germany. We have a dedicated site for Germany. This book presents an overview of antimicrobial peptides AMPs , their mechanisms of antimicrobial action, other activities, and various problems that must still be overcome regarding their clinical application. Divided into four major parts, the book begins with a general overview of AMPs Part I , and subsequently discusses the various mechanisms of antimicrobial action and methods for researching them Part 2.

    It then addresses a range of activities other than antimicrobial action, such as cell penetration, antisepsis, anticancer, and immunomodulatory activities Part 3 , and explores the prospects of clinical application from various standpoints such as the selective toxicity, design, and discovery of AMPs Part 4.

    A huge number of AMPs have been discovered in plants, insects, and vertebrates including humans, and constitute host defense systems against invading pathogenic microorganisms. Consequently, many attempts have been made to utilize AMPs as antibiotics.