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Journal articles on the topic 'Cationic antimicrobial peptides'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Bradshaw, Jeremy P. "Cationic Antimicrobial Peptides." BioDrugs 17, no. 4 (2003): 233–40. http://dx.doi.org/10.2165/00063030-200317040-00002.

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2

Ball, S. L., G. P. Siou, J. A. Wilson, A. Howard, B. H. Hirst, and J. Hall. "Expression and immunolocalisation of antimicrobial peptides within human palatine tonsils." Journal of Laryngology & Otology 121, no. 10 (2007): 973–78. http://dx.doi.org/10.1017/s0022215107006184.

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Background: Recurrent acute tonsillitis is one of the most frequent ENT referrals, yet its pathogenesis remains poorly understood, and tonsillectomy still costs the National Health Service more than £60 000 000 annually. Antimicrobial cationic peptides are components of the innate immune system. They are generally small, highly positively charged peptides with broad spectrum antimicrobial activity which function as the body's ‘natural antibiotics'. The role of antimicrobial cationic peptides in the susceptibility of patients to recurrent acute tonsillitis is unknown.Aims: To characterise and c

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3

Stark, Margareta, Li-Ping Liu, and Charles M. Deber. "Cationic Hydrophobic Peptides with Antimicrobial Activity." Antimicrobial Agents and Chemotherapy 46, no. 11 (2002): 3585–90. http://dx.doi.org/10.1128/aac.46.11.3585-3590.2002.

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ABSTRACT The MICs of cationic, hydrophobic peptides of the prototypic sequence KKAAAXAAAAAXAAWAAXAAAKKKK-amide (where X is one of the 20 commonly occurring amino acids) are in a low micromolar range for a panel of gram-negative and gram-positive bacteria, with no or low hemolytic activity against human and rabbit erythrocytes. The peptides are active only when the average segmental hydrophobicity of the 19-residue core is above an experimentally determined threshold value (where X is Phe, Trp, Leu, Ile, Met, Val, Cys, or Ala). Antimicrobial activity could be increased by using peptides that we

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4

Bechinger, B., and S. U. Gorr. "Antimicrobial Peptides: Mechanisms of Action and Resistance." Journal of Dental Research 96, no. 3 (2016): 254–60. http://dx.doi.org/10.1177/0022034516679973.

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More than 40 antimicrobial peptides and proteins (AMPs) are expressed in the oral cavity. These AMPs have been organized into 6 functional groups, 1 of which, cationic AMPs, has received extensive attention in recent years for their promise as potential antibiotics. The goal of this review is to describe recent advances in our understanding of the diverse mechanisms of action of cationic AMPs and the bacterial resistance against these peptides. The recently developed peptide GL13K is used as an example to illustrate many of the discussed concepts. Cationic AMPs typically exhibit an amphipathic

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5

Friedrich, Carol, Monisha G. Scott, Nedra Karunaratne, Hong Yan, and Robert E. W. Hancock. "Salt-Resistant Alpha-Helical Cationic Antimicrobial Peptides." Antimicrobial Agents and Chemotherapy 43, no. 7 (1999): 1542–48. http://dx.doi.org/10.1128/aac.43.7.1542.

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ABSTRACT Analogues based on the insect cecropin–bee melittin hybrid peptide (CEME) were studied and analyzed for activity and salt resistance. The new variants were designed to have an increase in amphipathic α-helical content (CP29 and CP26) and in overall positive charge (CP26). The α-helicity of these peptides was demonstrated by circular dichroism spectroscopy in the presence of liposomes. CP29 was shown to have activity against gram-negative bacteria that was similar to or better than those of the parent peptides, and CP26 had similar activity. CP29 had cytoplasmic membrane permeabilizati

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Zhang, Lijuan, and Timothy J. Falla. "Cationic antimicrobial peptides – an update." Expert Opinion on Investigational Drugs 13, no. 2 (2004): 97–106. http://dx.doi.org/10.1517/13543784.13.2.97.

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7

Brown, Kelly L., and Robert EW Hancock. "Cationic host defense (antimicrobial) peptides." Current Opinion in Immunology 18, no. 1 (2006): 24–30. http://dx.doi.org/10.1016/j.coi.2005.11.004.

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8

Ciumac, Daniela, Haoning Gong, Xuzhi Hu, and Jian Ren Lu. "Membrane targeting cationic antimicrobial peptides." Journal of Colloid and Interface Science 537 (March 2019): 163–85. http://dx.doi.org/10.1016/j.jcis.2018.10.103.

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9

Frecer, V., B. Ho, and J. L. Ding. "De Novo Design of Potent Antimicrobial Peptides." Antimicrobial Agents and Chemotherapy 48, no. 9 (2004): 3349–57. http://dx.doi.org/10.1128/aac.48.9.3349-3357.2004.

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ABSTRACT Lipopolysaccharide (LPS), shed by gram-negative bacteria during infection and antimicrobial therapy, may lead to lethal endotoxic shock syndrome. A rational design strategy based on the presumed mechanism of antibacterial effect was adopted to design cationic antimicrobial peptides capable of binding to LPS through tandemly repeated sequences of alternating cationic and nonpolar residues. The peptides were designed to achieve enhanced antimicrobial potency due to initial bacterial membrane binding with a reduced risk of endotoxic shock. The peptides designed displayed binding affiniti

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10

Walkenhorst, William F., J. Wolfgang Klein, Phuong Vo, and William C. Wimley. "pH Dependence of Microbe Sterilization by Cationic Antimicrobial Peptides." Antimicrobial Agents and Chemotherapy 57, no. 7 (2013): 3312–20. http://dx.doi.org/10.1128/aac.00063-13.

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ABSTRACTWe recently described a family of cationic antimicrobial peptides (CAMPs) selected from a combinatorial library that exhibited potent, broad-spectrum activity at neutral pH and low ionic strength. To further delimit the utility and activity profiles of these peptides, we investigated the effects of solution conditions, such as pH and ionic strength, on the efficacy of the peptide antimicrobials against a panel of microorganisms. Peptide minimum sterilizing concentrations (MSCs) varied linearly with pH for each subtype within our family of CAMPs for all organisms tested. The peptides we

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11

Oyston, P. C. F., M. A. Fox, S. J. Richards, and G. C. Clark. "Novel peptide therapeutics for treatment of infections." Journal of Medical Microbiology 58, no. 8 (2009): 977–87. http://dx.doi.org/10.1099/jmm.0.011122-0.

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As antibiotic resistance increases worldwide, there is an increasing pressure to develop novel classes of antimicrobial compounds to fight infectious disease. Peptide therapeutics represent a novel class of therapeutic agents. Some, such as cationic antimicrobial peptides and peptidoglycan recognition proteins, have been identified from studies of innate immune effector mechanisms, while others are completely novel compounds generated in biological systems. Currently, only selected cationic antimicrobial peptides have been licensed, and only for topical applications. However, research using ne

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12

Hwang, Peter M., and Hans J. Vogel. "Structure-function relationships of antimicrobial peptides." Biochemistry and Cell Biology 76, no. 2-3 (1998): 235–46. http://dx.doi.org/10.1139/o98-026.

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Antimicrobial peptides are ubiquitously produced throughout nature. Many of these relatively short peptides (6-50 residues) are lethal towards bacteria and fungi, yet they display minimal toxicity towards mammalian cells. All of the peptides are highly cationic and hydrophobic. It is widely believed that they act through nonspecific binding to biological membranes, even though the exact nature of these interactions is presently unclear. High-resolution nuclear magnetic resonance (NMR) has contributed greatly to knowledge in this field, providing insight about peptide structure in aqueous solut

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13

Scott, Monisha G., Hong Yan та Robert E. W. Hancock. "Biological Properties of Structurally Related α-Helical Cationic Antimicrobial Peptides". Infection and Immunity 67, № 4 (1999): 2005–9. http://dx.doi.org/10.1128/iai.67.4.2005-2009.1999.

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ABSTRACT A series of α-helical cationic antimicrobial peptide variants with small amino acid changes was designed. Alterations in the charge, hydrophobicity, or length of the variant peptides did not improve the antimicrobial activity, and there was no statistically significant correlation between any of these factors and the MIC forPseudomonas aeruginosa, Escherichia coli, orSalmonella typhimurium. Individual peptides demonstrated synergy with conventional antibiotics against antibiotic-resistant strains of P. aeruginosa. The peptides varied considerably in the ability to bind E. coli O111:B4

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14

Kuppusamy, Willcox, Black, and Kumar. "Short Cationic Peptidomimetic Antimicrobials." Antibiotics 8, no. 2 (2019): 44. http://dx.doi.org/10.3390/antibiotics8020044.

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The rapid growth of antimicrobial resistance against several frontline antibiotics has encouraged scientists worldwide to develop new alternatives with unique mechanisms of action. Antimicrobial peptides (AMPs) have attracted considerable interest due to their rapid killing and broad-spectrum activity. Peptidomimetics overcome some of the obstacles of AMPs such as high cost of synthesis, short half-life in vivo due to their susceptibility to proteolytic degradation, and issues with toxicity. This review will examine the development of short cationic peptidomimetics as antimicrobials.

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15

Ramón-García, Santiago, Ralf Mikut, Carol Ng, et al. "Targeting Mycobacterium tuberculosis and Other Microbial Pathogens Using Improved Synthetic Antibacterial Peptides." Antimicrobial Agents and Chemotherapy 57, no. 5 (2013): 2295–303. http://dx.doi.org/10.1128/aac.00175-13.

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ABSTRACTThe lack of effective therapies for treating tuberculosis (TB) is a global health problem. WhileMycobacterium tuberculosisis notoriously resistant to most available antibiotics, we identified synthetic short cationic antimicrobial peptides that were active at low micromolar concentrations (less than 10 μM). These small peptides (averaging 10 amino acids) had remarkably broad spectra of antimicrobial activities against both bacterial and fungal pathogens and an indication of low cytotoxicity. In addition, their antimicrobial activities displayed various degrees of species specificity th

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16

Anaya-López, José Luis, Joel Edmundo López-Meza, and Alejandra Ochoa-Zarzosa. "Bacterial resistance to cationic antimicrobial peptides." Critical Reviews in Microbiology 39, no. 2 (2012): 180–95. http://dx.doi.org/10.3109/1040841x.2012.699025.

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17

Vega, Luis Alberto, and Michael G. Caparon. "Cationic antimicrobial peptides disrupt theStreptococcus pyogenesExPortal." Molecular Microbiology 85, no. 6 (2012): 1119–32. http://dx.doi.org/10.1111/j.1365-2958.2012.08163.x.

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18

Hancock, Robert EW. "Cationic antimicrobial peptides: towards clinical applications." Expert Opinion on Investigational Drugs 9, no. 8 (2000): 1723–29. http://dx.doi.org/10.1517/13543784.9.8.1723.

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19

Tassanakajon, Anchalee, Piti Amparyup, Kunlaya Somboonwiwat, and Premruethai Supungul. "Cationic Antimicrobial Peptides in Penaeid Shrimp." Marine Biotechnology 12, no. 5 (2010): 487–505. http://dx.doi.org/10.1007/s10126-010-9288-9.

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20

Tassanakajon, Anchalee, Piti Amparyup, Kunlaya Somboonwiwat, and Premruethai Supungul. "Cationic Antimicrobial Peptides in Penaeid Shrimp." Marine Biotechnology 13, no. 4 (2011): 639–57. http://dx.doi.org/10.1007/s10126-011-9381-8.

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21

Serrano, Griselda N., George G. Zhanel та Frank Schweizer. "Antibacterial Activity of Ultrashort Cationic Lipo-β-Peptides". Antimicrobial Agents and Chemotherapy 53, № 5 (2009): 2215–17. http://dx.doi.org/10.1128/aac.01100-08.

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ABSTRACT Previously reported d,l-lipo-α-peptides and their lipo-β-peptide counterparts (C16-KGGK, C16-KAAK, C16-KKKK, and C12-KLLK) were studied, and the lipo-β-peptides were found to retain antimicrobial activity. Likewise, no significant changes in antimicrobial activity were found upon activity comparisons with d,l-amino acid-based lipopeptides or any l-amino acid lipopeptides. As a defined amphipathic structure is unlikely to form with such short molecules and as similar activities were obtained from all lipopeptides, we suspect that the action of membrane permeation is retained.

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22

Strandberg, Erik, Deniz Tiltak, Marco Ieronimo, Nathalie Kanithasen, Parvesh Wadhwani та Anne S. Ulrich. "Influence of C-terminal amidation on the antimicrobial and hemolytic activities of cationic α-helical peptides". Pure and Applied Chemistry 79, № 4 (2007): 717–28. http://dx.doi.org/10.1351/pac200779040717.

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The effect of C-terminal amidation on the antimicrobial and hemolytic activities of antimicrobial peptides was studied using three cationic peptides which form amphiphilic α-helices when bound to membranes. The natural antimicrobial peptide PGLa, the designer-made antibiotic MSI-103, and the cell-penetrating "model amphipathic peptide" (MAP) are all amidated in their original forms, and their biological activities were compared with the same sequences carrying a free C-terminus. It was found that, in general, a free COOH-terminus reduces both the antimicrobial activity and the hemolytic side e

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23

Amirkhanov, N. V., N. V. Tikunova, and D. V. Pyshnyi. "Synthetic Antimicrobial Peptides: I. Antimicrobial Activity of Amphiphilic and Nonamphiphilic Cationic Peptides." Russian Journal of Bioorganic Chemistry 44, no. 5 (2018): 492–503. http://dx.doi.org/10.1134/s1068162018050035.

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24

Deslouches, Berthony, Shruti M. Phadke, Vanja Lazarevic, et al. "De Novo Generation of Cationic Antimicrobial Peptides: Influence of Length and Tryptophan Substitution on Antimicrobial Activity." Antimicrobial Agents and Chemotherapy 49, no. 1 (2005): 316–22. http://dx.doi.org/10.1128/aac.49.1.316-322.2005.

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ABSTRACT Comparison of human immunodeficiency virus lentiviral lytic peptide 1 with other host-derived peptides indicates that antimicrobial properties of membrane-active peptides are markedly influenced by their cationic, hydrophobic, and amphipathic properties. Many common themes, such as Arg composition of the cationic face of an amphipathic helix and the importance of maintaining the hydrophobic face, have been deduced from these observations. These studies suggest that a peptide with these structural properties can be derived de novo by using only a few strategically positioned amino acid

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25

Hilpert, Kai, Brett McLeod, Jessie Yu, et al. "Short Cationic Antimicrobial Peptides Interact with ATP." Antimicrobial Agents and Chemotherapy 54, no. 10 (2010): 4480–83. http://dx.doi.org/10.1128/aac.01664-09.

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ABSTRACT The mode of action of short, nonhelical antimicrobial peptides is still not well understood. Here we show that these peptides interact with ATP and directly inhibit the actions of certain ATP-dependent enzymes, such as firefly luciferase, DnaK, and DNA polymerase. α-Helical and planar or circular antimicrobial peptides did not show such interaction with ATP.

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26

Bagheri, Mojtaba, Michael Beyermann, and Margitta Dathe. "Immobilization Reduces the Activity of Surface-Bound Cationic Antimicrobial Peptides with No Influence upon the Activity Spectrum." Antimicrobial Agents and Chemotherapy 53, no. 3 (2008): 1132–41. http://dx.doi.org/10.1128/aac.01254-08.

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ABSTRACT Early studies of immobilized peptides mainly focused upon the relationship between structural properties and the activity of soluble and surface-tethered sequences. The intention of this study was to analyze the influence of immobilization parameters upon the activity profile of peptides. Resin beads (TentaGel S NH2, HypoGel 400 NH2, and HypoGel 200 NH2) with polyethylene glycol spacers of different lengths were rendered antimicrobial by linkage of an amphipathic model KLAL peptide and magainin-derived MK5E. Standard solid-phase peptide synthesis, thioalkylation, and ligation strategi

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27

Cytryńska, Małgorzata, and Agnieszka Zdybicka-Barabas. "Defense peptides: recent developments." Biomolecular Concepts 6, no. 4 (2015): 237–51. http://dx.doi.org/10.1515/bmc-2015-0014.

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AbstractDefense peptides are small amphipathic molecules that exhibit antimicrobial, antitumor, antiviral, and immunomodulatory properties. This review summarizes current knowledge on the mechanisms of antimicrobial activity of cationic and anionic defense peptides, indicating peptide-based as well as microbial cell-based factors affecting this activity. The peptide-based factors include charge, hydrophibicity, and amphipathicity, whereas the pathogen-based factors are membrane lipid composition, presence of sterols, membrane fluidity, cell wall components, and secreted factors such as extrace

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Amirkhanov, N. V., A. V. Bardasheva, N. V. Tikunova, and D. V. Pyshnyi. "Synthetic Antimicrobial Peptides: III—Effect of Cationic Groups of Lysine, Arginine, and Histidine on Antimicrobial Activity of Peptides with a Linear Type of Amphipathicity." Russian Journal of Bioorganic Chemistry 47, no. 3 (2021): 681–90. http://dx.doi.org/10.1134/s106816202103002x.

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Abstract We have studied the antimicrobial and hemolytic activity of synthetic antimicrobial peptides (SAMPs), i.e., Arg9Phe2 (P1-Arg), Lys9Phe2 (P2-Lys), and His9Phe2 (P3-His), which have a “linear” type of amphipathicity and contain the cationic amino acid residues of arginine, lysine, or histidine. In this study, we have used various pathogenic microorganism strains of gram-negative bacteria (Pseudomonas aeruginosa, Escherichia coli, and Salmonella enterica), gram-positive bacteria (Staphylococcus aureus), and the conditionally pathogenic yeast fungus (Candida albicans). It has been shown t

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Anne Pereira, H. "Novel Therapies Based on Cationic Antimicrobial Peptides." Current Pharmaceutical Biotechnology 7, no. 4 (2006): 229–34. http://dx.doi.org/10.2174/138920106777950771.

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30

Brouwer, Carlo P. J. M., Marty Wulferink, and Mick M. Welling. "The Pharmacology of Radiolabeled Cationic Antimicrobial Peptides." Journal of Pharmaceutical Sciences 97, no. 5 (2008): 1633–51. http://dx.doi.org/10.1002/jps.21034.

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31

Andres, E., and J. L. Dimarcq. "Cationic antimicrobial peptides: update of clinical development." Journal of Internal Medicine 255, no. 4 (2004): 519–20. http://dx.doi.org/10.1046/j.1365-2796.2003.01278.x.

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32

Park, Ho Jin, Ki Mo Kang, Kevin Dybvig, Bok Luel Lee, Yong Woo Jung, and In Hee Lee. "Interaction of cationic antimicrobial peptides withMycoplasma pulmonis." FEBS Letters 587, no. 20 (2013): 3321–26. http://dx.doi.org/10.1016/j.febslet.2013.08.016.

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33

Jin, Yi, Janet Hammer, Michelle Pate та ін. "Antimicrobial Activities and Structures of Two Linear Cationic Peptide Families with Various Amphipathic β-Sheet and α-Helical Potentials". Antimicrobial Agents and Chemotherapy 49, № 12 (2005): 4957–64. http://dx.doi.org/10.1128/aac.49.12.4957-4964.2005.

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ABSTRACT Many naturally occurring antimicrobial peptides comprise cationic linear sequences with the potential to adopt an amphipathic α-helical conformation. We designed a linear 18-residue peptide that adopted an amphipathic β-sheet structure when it was bound to lipids. In comparison to a 21-residue amphipathic α-helical peptide of equal charge and hydrophobicity, this peptide possessed more similar antimicrobial activity and greater selectivity in binding to and inducing leakage in vesicles composed of bacterial membrane lipids than vesicles composed of mammalian membrane lipids (J. Blazyk

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Winfred, Sofi Beaula, Gowri Meiyazagan, Jiban J. Panda, et al. "Antimicrobial activity of cationic peptides in endodontic procedures." European Journal of Dentistry 08, no. 02 (2014): 254–60. http://dx.doi.org/10.4103/1305-7456.130626.

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ABSTRACT Objectives: The present study aimed to investigate the antimicrobial and biofilm inhibition activity of synthetic antimicrobial peptides (AMPs) against microbes such as Enterococcus faecalis, Staphylococcus aureus, and Candida albicans which are involved in endodontic infections. Materials and Methods: Agar diffusion test was done to determine the activity of peptides. The morphological changes in E. faecalis and reduction in biofilm formation after treatment with peptides were observed using scanning electron microscope. The efficacy of peptides using an ex vivo dentinal model was de

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35

Paterson, David J., Manlio Tassieri, Julien Reboud, Rab Wilson, and Jonathan M. Cooper. "Lipid topology and electrostatic interactions underpin lytic activity of linear cationic antimicrobial peptides in membranes." Proceedings of the National Academy of Sciences 114, no. 40 (2017): E8324—E8332. http://dx.doi.org/10.1073/pnas.1704489114.

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Linear cationic antimicrobial peptides are a diverse class of molecules that interact with a wide range of cell membranes. Many of these peptides disrupt cell integrity by forming membrane-spanning pores that ultimately lead to their death. Despite these peptides high potency and ability to evade acquired bacterial drug resistance, there is a lack of knowledge on their selectivity and activity mechanisms. Such an understanding would provide an informative framework for rational design and could lead to potential antimicrobial therapeutic targets. In this paper, we use a high-throughput microfl

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Evans, Ellen W., and Barry G. Harmon. "A Review of Antimicrobial Peptides: Defensins and Related Cationic Peptides." Veterinary Clinical Pathology 24, no. 4 (1995): 109–16. http://dx.doi.org/10.1111/j.1939-165x.1995.tb00949.x.

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37

Harm, Stephan, Karl Lohner, Ute Fichtinger, Claudia Schildböck, Jennifer Zottl, and Jens Hartmann. "Blood Compatibility—An Important but Often Forgotten Aspect of the Characterization of Antimicrobial Peptides for Clinical Application." International Journal of Molecular Sciences 20, no. 21 (2019): 5426. http://dx.doi.org/10.3390/ijms20215426.

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Acylation of antimicrobial peptides mimics the structure of the natural lipopeptide polymyxin B, and increases antimicrobial and endotoxin-neutralizing activities. In this study, the antimicrobial properties of lactoferrin-based LF11 peptides as well as blood compatibility as a function of acyl chain length were investigated. Beyond the classical hemolysis test, the biocompatibility was determined with human leukocytes and platelets, and the influence of antimicrobial peptides (AMPs) on the plasmatic coagulation and the complement system was investigated. The results of this study show that th

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Fernández, Lucía, W. James Gooderham, Manjeet Bains, Joseph B. McPhee, Irith Wiegand, and Robert E. W. Hancock. "Adaptive Resistance to the “Last Hope” Antibiotics Polymyxin B and Colistin in Pseudomonas aeruginosa Is Mediated by the Novel Two-Component Regulatory System ParR-ParS." Antimicrobial Agents and Chemotherapy 54, no. 8 (2010): 3372–82. http://dx.doi.org/10.1128/aac.00242-10.

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ABSTRACT As multidrug resistance increases alarmingly, polymyxin B and colistin are increasingly being used in the clinic to treat serious Pseudomonas aeruginosa infections. In this opportunistic pathogen, subinhibitory levels of polymyxins and certain antimicrobial peptides induce resistance toward higher, otherwise lethal, levels of these antimicrobial agents. It is known that the modification of lipid A of lipopolysaccharide (LPS) is a key component of this adaptive peptide resistance, but to date, the regulatory mechanism underlying peptide regulation in P. aeruginosa has remained elusive.

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Silva, Sara, and Nuno Vale. "Cationic Antimicrobial Peptides for Tuberculosis: A Mini-Review." Current Protein & Peptide Science 20, no. 9 (2019): 885–92. http://dx.doi.org/10.2174/1389203720666190626160057.

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Cationic antimicrobial peptides (CAMPs) can be considered as new potential therapeutic agents for Tuberculosis treatment with a specific amino acid sequence. New studies can be developed in the future to improve the pharmacological properties of CAMPs and also understand possible resistance mechanisms. This review discusses the principal properties of natural and/or synthetic CAMPs, and how these new peptides have a significant specificity for Mycobacterium tuberculosis. Also, we propose some alternative strategies to enhance the therapeutic activity of these CAMPs that include coadministratio

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De-Simone, Salvatore G., Andre L. A. Souza, Jorge L. S. Pina, Ivan N. Junior, Maria C. Lourenço, and David W. Provance. "Bactericidal Activity of a Cationic Peptide on Neisseria meningitidis." Infectious Disorders - Drug Targets 19, no. 4 (2019): 421–27. http://dx.doi.org/10.2174/1871526518666180816132414.

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Background: The increasing prevalence of antibiotic resistant bacteria has raised an urgent need for substitute remedies. Antimicrobial peptides (AMPs) are considered promising candidates to address infections by multidrug-resistant bacteria through new mechanisms of action that require a careful evaluation of their performance. Objective: Identification of effective AMPs against Neisseria meningitidis, which represents a pathogen of great public health importance worldwide that is intrinsically resistant to some AMPs, such as polymyxin B. Methods: A cationic 11-residue peptide (KLKLLLLLKLK),

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Kilelee, Erin, Antje Pokorny, Michael R. Yeaman, and Arnold S. Bayer. "Lysyl-Phosphatidylglycerol Attenuates Membrane Perturbation Rather than Surface Association of the Cationic Antimicrobial Peptide 6W-RP-1 in a Model Membrane System: Implications for Daptomycin Resistance." Antimicrobial Agents and Chemotherapy 54, no. 10 (2010): 4476–79. http://dx.doi.org/10.1128/aac.00191-10.

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ABSTRACT The presence of the cationic phospholipid lysyl-phosphatidylglycerol (lysyl-PG) in staphylococcal cytoplasmic membranes has been linked to increased resistance to cationic compounds, including antibiotics such as daptomycin as well as host defense antimicrobial peptides. We investigated the effects of lysyl-PG on binding of 6W-RP-1, a synthetic antimicrobial peptide, to lipid vesicles and on peptide-induced membrane permeabilization. Unexpectedly, physiological lysyl-PG concentrations only minimally reduced membrane binding of 6W-RP-1. In contrast, 6W-RP-1-induced dye leakage was seve

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Thwaite, Joanne E., Suzanne Humphrey, Marc A. Fox, et al. "The cationic peptide magainin II is antimicrobial for Burkholderia cepacia-complex strains." Journal of Medical Microbiology 58, no. 7 (2009): 923–29. http://dx.doi.org/10.1099/jmm.0.008128-0.

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This study was undertaken to determine the antibacterial activity of eight cationic antimicrobial peptides towards strains of genomovars I–V of the Burkholderia cepacia complex (Bcc) in time–kill assays. All but one of the peptides failed to show activity against the panel of test strains. The exception was magainin II, a 23 aa peptide isolated from the epidermis of the African clawed frog, Xenopus laevis, which exhibited significant bactericidal activity for Bcc genomovars most frequently associated with lung infection of patients with cystic fibrosis. In vitro studies indicated that magainin

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Jean, Catherine, Martine Boulianne, Michel Britten, and Gilles Robitaille. "Antimicrobial activity of buttermilk and lactoferrin peptide extracts on poultry pathogens." Journal of Dairy Research 83, no. 4 (2016): 497–504. http://dx.doi.org/10.1017/s0022029916000637.

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Antibiotics are commonly used in poultry feed as growth promoters. This practice is questioned given the arising importance of antibiotic resistance. Antimicrobial peptides can be used as food additives for a potent alternative to synthetic or semi-synthetic antibiotics. The objective of this study was to develop a peptide production method based on membrane adsorption chromatography in order to produce extracts with antimicrobial activity against avian pathogens (Salmonella entericavar. Enteritidis,Salmonella entericavar. Typhimurium, and twoEscherichia colistrains, O78:H80 and TK3 O1:K1) as

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Henriques, Sónia Troeira, Manuel Nuno Melo, and Miguel A. R. B. Castanho. "Cell-penetrating peptides and antimicrobial peptides: how different are they?" Biochemical Journal 399, no. 1 (2006): 1–7. http://dx.doi.org/10.1042/bj20061100.

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Some cationic peptides, referred to as CPPs (cell-penetrating peptides), have the ability to translocate across biological membranes in a non-disruptive way and to overcome the impermeable nature of the cell membrane. They have been successfully used for drug delivery into mammalian cells; however, there is no consensus about the mechanism of cellular uptake. Both endocytic and non-endocytic pathways are supported by experimental evidence. The observation that some AMPs (antimicrobial peptides) can enter host cells without damaging their cytoplasmic membrane, as well as kill pathogenic agents,

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Yan, Hong, and Robert E. W. Hancock. "Synergistic Interactions between Mammalian Antimicrobial Defense Peptides." Antimicrobial Agents and Chemotherapy 45, no. 5 (2001): 1558–60. http://dx.doi.org/10.1128/aac.45.5.1558-1560.2001.

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ABSTRACT A single animal can express several cationic antimicrobial peptides with different sequences and structures. We demonstrate that mammalian peptides from different structural classes frequently show synergy with each other and selectively show synergy with human lysozyme.

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Ginsburg, Isaac, and Erez Koren. "Are cationic antimicrobial peptides also ‘double-edged swords’?" Expert Review of Anti-infective Therapy 6, no. 4 (2008): 453–62. http://dx.doi.org/10.1586/14787210.6.4.453.

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Wenzel, M., A. I. Chiriac, A. Otto, et al. "Small cationic antimicrobial peptides delocalize peripheral membrane proteins." Proceedings of the National Academy of Sciences 111, no. 14 (2014): E1409—E1418. http://dx.doi.org/10.1073/pnas.1319900111.

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Zhang, Lijuan, Annett Rozek, and Robert E. W. Hancock. "Interaction of Cationic Antimicrobial Peptides with Model Membranes." Journal of Biological Chemistry 276, no. 38 (2001): 35714–22. http://dx.doi.org/10.1074/jbc.m104925200.

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Brogden, K. A., M. Ackermann, and K. M. Huttner. "Small, anionic, and charge-neutralizing propeptide fragments of zymogens are antimicrobial." Antimicrobial Agents and Chemotherapy 41, no. 7 (1997): 1615–17. http://dx.doi.org/10.1128/aac.41.7.1615.

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Some inactive precursor proteins, or zymogens, contain small, amino terminus, homopolymeric regions of Asp that neutralize the cationic charge of the active protein during synthesis. After posttranslational cleavage, the anionic propeptide fragment may exhibit antimicrobial activity. To demonstrate this, ovine trypsinogen activation peptide, and frog (Xenopus laevis) PYL activation peptide, both containing homopolymeric regions of Asp, were synthesized and tested against previously described surfactant-associated anionic peptide. Peptides inhibited the growth of both gram-negative (MIC, 0.08 t

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Midura-Nowaczek, Krystyna, and Agnieszka Markowska. "Antimicrobial Peptides and Their Analogs: Searching for New Potential Therapeutics." Perspectives in Medicinal Chemistry 6 (January 2014): PMC.S13215. http://dx.doi.org/10.4137/pmc.s13215.

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Antimicrobial peptides (AMPs) are an essential part of innate immunity. These compounds have been considered as potential therapeutics because of their broad-spectrum activities and proven ability to avoid antimicrobial resistance, but their clinical and commercial developments have some limitations, such as susceptibility to proteases and a high cost of peptide production. To overcome these problems, many researchers have tried to develop short active peptides, their modifications and mimics with better properties while retaining their basic features of natural AMPs such as cationic charge an

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