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Academic literature on the topic 'Cationic Amphiphilic Peptides'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Cationic Amphiphilic Peptides"

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Silva Nigenda, Ezequiel, Tobias M. Postma, Mohammed Hezwani, Alin Pirvan, Susan Gannon, Carol-Anne Smith, Mathis Riehle, and Rob M. J. Liskamp. "Synthesis and cellular penetration properties of new phosphonium based cationic amphiphilic peptides." MedChemComm 9, no. 6 (2018): 982–87. http://dx.doi.org/10.1039/c8md00113h.

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Akkarawongsa, Radeekorn, Terra B. Potocky, Emily P. English, Samuel H. Gellman, and Curtis R. Brandt. "Inhibition of Herpes Simplex Virus Type 1 Infection by Cationic β-Peptides." Antimicrobial Agents and Chemotherapy 52, no. 6 (April 7, 2008): 2120–29. http://dx.doi.org/10.1128/aac.01424-07.

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ABSTRACT Previously, it was shown that cationic α-peptides derived from the human immunodeficiency virus TAT protein transduction domain blocked herpes simplex virus type 1 (HSV-1) entry. We now show that cationic oligomers of β-amino acids (“β-peptides”) inhibit HSV-1 infection. Among three cationic β-peptides tested, the most effective inhibition was observed for the one with a strong propensity to adopt a helical conformation in which cationic and hydrophobic residues are segregated from one another (“globally amphiphilic helix”). The antiviral effect was not cell type specific. Inhibition of virus infection by the β-peptides occurred at the postattachment penetration step, with a 50% effective concentration of 3 μM for the most-effective β-peptide. The β-peptides did not inactivate virions in solution, nor did they induce resistance to infection when cells were pretreated with the β-peptides. The β-peptides showed little if any toxicity toward Vero cells. These results raise the possibility that cationic β-peptides may be useful antiviral agents for HSV-1 and demonstrate the potential of β-peptides as novel antiviral drugs.
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Schweizer, Frank. "Cationic amphiphilic peptides with cancer-selective toxicity." European Journal of Pharmacology 625, no. 1-3 (December 2009): 190–94. http://dx.doi.org/10.1016/j.ejphar.2009.08.043.

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Findlay, Brandon, George G. Zhanel, and Frank Schweizer. "Cationic Amphiphiles, a New Generation of Antimicrobials Inspired by the Natural Antimicrobial Peptide Scaffold." Antimicrobial Agents and Chemotherapy 54, no. 10 (August 9, 2010): 4049–58. http://dx.doi.org/10.1128/aac.00530-10.

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ABSTRACT Naturally occurring cationic antimicrobial peptides (AMPs) and their mimics form a diverse class of antibacterial agents currently validated in preclinical and clinical settings for the treatment of infections caused by antimicrobial-resistant bacteria. Numerous studies with linear, cyclic, and diastereomeric AMPs have strongly supported the hypothesis that their physicochemical properties, rather than any specific amino acid sequence, are responsible for their microbiological activities. It is generally believed that the amphiphilic topology is essential for insertion into and disruption of the cytoplasmic membrane. In particular, the ability to rapidly kill bacteria and the relative difficulty with which bacteria develop resistance make AMPs and their mimics attractive targets for drug development. However, the therapeutic use of naturally occurring AMPs is hampered by the high manufacturing costs, poor pharmacokinetic properties, and low bacteriological efficacy in animal models. In order to overcome these problems, a variety of novel and structurally diverse cationic amphiphiles that mimic the amphiphilic topology of AMPs have recently appeared. Many of these compounds exhibit superior pharmacokinetic properties and reduced in vitro toxicity while retaining potent antibacterial activity against resistant and nonresistant bacteria. In summary, cationic amphiphiles promise to provide a new and rich source of diverse antibacterial lead structures in the years to come.
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Kaconis, Yani, Ina Kowalski, Jörg Howe, Annemarie Brauser, Walter Richter, Iosu Razquin-Olazarán, Melania Iñigo-Pestaña, et al. "Biophysical Mechanisms of Endotoxin Neutralization by Cationic Amphiphilic Peptides." Biophysical Journal 100, no. 11 (June 2011): 2652–61. http://dx.doi.org/10.1016/j.bpj.2011.04.041.

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Cao, Meiwen, Yuming Wang, Xin Ge, Changhai Cao, Jing Wang, Hai Xu, Daohong Xia, Xiubo Zhao, and Jian R. Lu. "Effects of Anions on Nanostructuring of Cationic Amphiphilic Peptides." Journal of Physical Chemistry B 115, no. 41 (October 20, 2011): 11862–71. http://dx.doi.org/10.1021/jp205987w.

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Wiradharma, Nikken, Ulung Khoe, Charlotte A. E. Hauser, See Voon Seow, Shuguang Zhang, and Yi-Yan Yang. "Synthetic cationic amphiphilic α-helical peptides as antimicrobial agents." Biomaterials 32, no. 8 (March 2011): 2204–12. http://dx.doi.org/10.1016/j.biomaterials.2010.11.054.

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Kundu, Rajen. "Cationic Amphiphilic Peptides: Synthetic Antimicrobial Agents Inspired by Nature." ChemMedChem 15, no. 20 (September 8, 2020): 1887–96. http://dx.doi.org/10.1002/cmdc.202000301.

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Rideout, Darryl C., Michael Lambert, Debra A. Kendall, Gregory R. Moe, David G. Osterman, H. P. Tao, I. Bernard Weinstein, and E. T. Kaiser. "Amphiphilic cationic peptides mediate cell adhesion to plastic surfaces." Journal of Cellular Physiology 124, no. 3 (September 1985): 365–71. http://dx.doi.org/10.1002/jcp.1041240302.

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Strandberg, Erik, Deniz Tiltak, Marco Ieronimo, Nathalie Kanithasen, Parvesh Wadhwani, and Anne S. Ulrich. "Influence of C-terminal amidation on the antimicrobial and hemolytic activities of cationic α-helical peptides." Pure and Applied Chemistry 79, no. 4 (January 1, 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 effects of the peptides. The only exception was observed for MSI-103, whose antimicrobial activity was not decreased in the acid form. Having shown that the therapeutic index (TI) of this novel peptide is significantly higher than for the other tested peptides, with high antibiotic activity and little undesired effects, we suggest that it could be a useful starting point for further development of new peptide antibiotics.
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Dissertations / Theses on the topic "Cationic Amphiphilic Peptides"

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Reijmar, Brunnström Karin. "Development of lipodisks as carriers for cationic amphiphilic peptides." Doctoral thesis, Uppsala universitet, Analytisk kemi, 2016. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-305443.

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Antibiotics have made a tremendous contribution to mankind. They are one of the most successful medicines in human history. However, more and more bacterial strains develop resistance and the risk to public health can hardly be overstated. New types of antibiotics are urgently needed. Antimicrobial peptides (AMPs) have emerged as potential antibiotics because of their broad-spectrum activities and non-conventional mechanism of action. More recently, they have also received attention as promising anticancer agents. The clinical and commercial development of AMPs as a new generation of antibiotics and anticancer drugs is hampered, however, by issues concerning the toxicity, specificity and stability of the peptides. The aim of this thesis has been to explore if formulation in a novel type of nanocarriers, referred to as lipodisks, can be used to increase the therapeutic potential of AMPs as antimicrobial and anticancer agents. Focus has been on AMPs classified as cationic amphiphilic peptides. Encouragingly, the data presented suggests that the therapeutic potential of the AMP melittin as an antimicrobial and anticancer agent can be substantially increased by formulation in lipodisks. When formulated in the lipodisk, melittin is protected against enzymatic degradation. The lipodisk also offer a slow-release effect that sustains the bacterial cell-killing effect. We also show that specific delivery of melittin to tumour cells can be obtained by formulating the peptide in small EGF-targeting lipodisks. Melittin contains a tryptophan residue and its interaction with lipodisks can be characterized by means of fluorimetric binding assays. In order to investigate the binding behavior also for peptides that lack intrinsic fluorescence, we developed a method based on measurements using the QCM-D technique. Studies using this, and other techniques, confirmed that it is a general behavior for cationic amphiphilic peptides to preferentially bind to the highly curved rim of lipodisks. Results of our binding studies show that the peptide to lipid ratio in the lipodisks can be tuned and optimized by varying the size and charge of the disks. Taken together, the findings in this thesis point towards PEG-stabilized lipodisks as promising nanocarriers for antibacterial and anticancer peptides.
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Silva, Nigenda Ezequiel. "Synthesis of drug delivery systems based on pantothenic acid and cationic amphiphilic peptides modifications." Thesis, University of Glasgow, 2017. http://theses.gla.ac.uk/8917/.

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The constant problems encountered in the fields of medicinal and pharmaceutical chemistry, especially those related to the side effects of drug candidates, have risen the concern of developing methods that can help us achieve the therapeutic effect without undesired properties. This thesis describes the development of two different Drug Delivery Systems based on the modification of natural occurring molecules. The first one is directed to the treatment of parasitic tropical diseases. The alteration of pantothenic acid with the introduction of a double bond has proved to increase the uptake of fluorescent labelled molecules in different model systems with low cytotoxicity. The concept of this Drug Delivery System relies on the necessity of the parasites to consume the host’s pantothenic acid for their own biological processes. Due to their inability to synthesise this vitamin along with the huge supply they need to survive, it was hypothesised that the increased uptake of CJ-15,801 would allow us to attach interesting molecules that could be selectively delivered into parasites. The second example of a Drug Delivery System presented in this work is based on peptides released by cells of the immune system. The so called Cationic Amphiphilic Peptides are released by an organism that is under the attack of potential pathogens. Due to their physicochemical properties, they can stop an infection by direct killing of microorganisms by different mechanisms. Either by the membrane disruption or internalisation and intracellular targeting, the presence of positively charged residues play a major role on the activity of these peptides. By substitution of the natural occurring lysine and arginine residues with a new class of phosphonium based amino acids, a new class of cationic amphiphilic peptides was synthesised. Fluorescent versions of these peptides have allowed us to investigate their properties. They are characterised by their ability to cross cellular membranes with relatively low toxicity compared to the natural occurring versions of the sequences and even though their direct antimicrobial activity is diminished they can be used as potential Cell Penetrating Peptides. Finally, due to the nature of the cation present in these new peptides, it is theorised that they can have certain selectivity to deliver drugs into mitochondria. Although further studies to prove this need to be done, an initial experiment is reported at the end of this work.
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Findlay, Brandon. "Design and synthesis of cationic amphiphiles." American Society for Microbiology, 2010. http://hdl.handle.net/1993/21708.

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Cationic antimicrobial peptides (CAMPs) are produced by plants, animals and bacteria to protect their host against antagonistic microbes. The antitheses of selective antibiotics, these peptides are drawn by electrostatic and hydrophobic interactions to targets as diverse as the bacterial membrane, nucleic acids and serum proteins. This lack of specificity is their greatest strength, as mutations to single genes rarely lead to bacterial resistance. Resistance may be conferred by large scale alterations in cell envelope composition, which generally reduces bacterial fitness in the absence of peptide. Clinical applications of natural CAMPs are limited, as the peptides are toxic to mammalian cells and rapidly inactivated in vivo by serum albumin and proteases. Faced with these challenges we have prepared a number of CAMP analogues, with the goal of creating lead compounds for further development of antibacterial therapeutics. Much of our work has focused on ultrashort lipopeptides and lipopeptoids, which have properties similar to natural CAMPs and extremely abbreviated sequences. The simple structure of these scaffolds allows rapid creation of CAMP analogues in a brief period of time, allowing us to rapidly explore the structural requirements for CAMP activity. The balance of this work focuses on imparting CAMP-like behaviour to known antibiotics, in order to expand their spectrum of susceptible bacteria and combat the development of drug-resistant bacteria. In particular, the aminoglycosides neomycin and tobramycin have been fused to phenolic disinfectants such as triclosan and biclotymol, in order to improve their diffusion across the bacterial envelope and activity against Gram-negative bacteria.
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Shyam, Radhe. "Cationic amphipathic peptoid oligomers as antimicrobial peptide mimics." Thesis, Université Clermont Auvergne‎ (2017-2020), 2018. http://www.theses.fr/2018CLFAC048/document.

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Les organismes vivants produisent des peptides antimicrobiens (PAMs) pour se protéger contre les microbes. La résistance croissante aux antibiotiques nécessite le développement de nouvelles stratégies thérapeutiques et les PAMs sont des candidats prometteurs pour résoudre ce problème. Ils possèdent une activité à large spectre et leur principal mécanisme d'action par perméation de la membrane engendre peu de phénomènes de résistance. Néanmoins, leur faible biodisponibilité empêche leur utilisation. Certaines limitations peuvent être surmontées en développant des mîmes de PAMs qui conservent leur activité mais avec un potentiel thérapeutique accru. Les peptoïdes (oligomères de N-alkylglycine) structurés en hélice cationique amphiphile sont de bons mimes de PAMs. Les peptoïdes sont plus flexibles que les peptides en raison de l'isomérie cis/trans des amides N,N-disubstitués ; cependant la conformation des amides peut être contrôlée par un choix judicieux des chaînes latérales. Le but de cette thèse est d'étudier l'influence de chaînes latérales(hydrophobes ou cationiques) bloquant la conformation des amides en cis et induisant une structure hélicoïdale de type PolyProline I (PPI) robuste, sur l’activité antibactérienne et la sélectivité de peptoïdes. La conception, la synthèse et l’étude conformationnelle de nouveaux oligomères peptoïdes cationiques portant des chaînes latérales de type tert-butyle et/ou triazolium ont été réalisées. Dans un premier temps, la synthèse en solution d'oligomères à base de tert-butyle a été développée puis une stratégie de synthèse en phase solide a été mise en place pour accéder aux oligomères à base de 1,2,3-triazolium. Ensuite, ces nouveaux oligomères ont été évalués pour leur activité vis à vis d’un panel de bactéries Gram-positive et Gram-négative, leur l'activité antibiofilm et leur sélectivité cellulaire. Enfin, pour visualiser les effets des peptoïdes amphiphiles sur les bactéries, une étude de microscopie a été réalisée
Living organisms produce antimicrobial peptides (AMPs) to protect themselves against microbes.The growing problem of antimicrobial resistance calls for new therapeutic strategies and the natural AMPs have shown ground-breaking potential to address that issue. They show broad-spectrum activity and their main mechanism of action by bacterial cell membrane disruption implies low emergence of resistance which makes them potent candidates for replacing conventional antibiotics. Nevertheless, few hurdles are impeding their use, notably poor bioavailability profile. Some of these limitations can be overcome by developing peptidomimetics of AMPs which exhibit antibacterial activities together with enhanced therapeutic potential. Peptoids (i.e. N-alkyl glycine oligomers) adopting cationic amphipathic helical structures are mostly competent AMP mimetics. From a conformational point of view, peptoids are fundamentally more flexible than peptides primarily due to the cis/trans isomerism of N,N-disubstituted amides but studies in this area have shown that cis amide conformation can be controlled by careful choice of side-chain to set a PolyProline I-type helical structure of peptoids. In this thesis, the genesis of novel amphipathic cationic peptoids carrying cis-directing tert-butyl and/or triazolium-type side-chains and their untapped potential to act against bacteria will be discussed comprehensively. First, the solutionphase synthesis of tert-butyl-based oligomers was developed. Second, novel method of solid-phase submonomer synthesis was optimised to access 1,2,3-triazolium-based oligomers. Then, the synthesised cationic oligomers were evaluated for their antibacterial potential, followed by antibiofilm activity and cell selectivity assays. In the end, to have insights on the mode of action of amphipathic peptoids, microscopy was carried out
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Ahmad, Roni Oda Reiko. "Oligo-peptides confinés à la surface de membranes d'amphiphiles cationiques." S. l. : Bordeaux 1, 2008. http://ori-oai.u-bordeaux1.fr/pdf/2008/AHMAD_RONI_2008.pdf.

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Ahmad, Roni. "Oligo-peptides confinés à la surface de membranes d'amphiphiles cationiques." Thesis, Bordeaux 1, 2008. http://www.theses.fr/2008BOR13697/document.

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Les molécules amphiphiles sont dotées de propriétés d’auto-organisation en solution, conduisant à une grande variété de structures que l’on peut moduler en ajustant des paramètres moléculaires. Nous nous intéressons en particulier à des amphiphiles cationiques, dont nous faisons varier la nature du contre-ion. L’utilisation de contre-ions chiraux alanine à ainsi permis de conduire à l’apparition de structures supramoléculaires chirales, dont nous avons cherché à comprendre et contrôler la formation. Des contre-ion peptidique ont également été confinés à la surface d’assemblage des ces amphiphiles, induisant des structures secondaires particulières et la formation de structures chirales elles aussi remarquables
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(10010291), Samantha Mae Zeiders. "EXPLORING ANTIBIOTIC CONJUGATION TO CATIONIC AMPHIPHILIC POLYPROLINE HELICES." Thesis, 2021.

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Pathogenic bacteria present a critical threat to modern medicine. Therapeutic strategies to target and eliminate resilient bacteria are not advancing at the same rate as the emergence of bacterial resistance. An associated urgent concern regarding antibiotic resistance is the existence and proliferation of intracellular bacteria, which find refuge from bactericidal mechanisms by hiding within mammalian cells. Therefore, many once-successful antibiotics become ineffective through the development of resistance, or through failure to reach intracellular locations in therapeutic concentration. To overcome these challenges, the covalent combination of a conventional antibiotic with an antibiotic, cell-penetrating peptide was explored to develop dual-action antibiotic conjugates.

Herein, we utilized a strategy in conjugating the antibiotics by a cleavable linkage to cationic amphiphilic polyproline helices (CAPHs) to improve vancomycin and linezolid antibiotics. This approach enables the conjugate to penetrate cells and deliver two potent monomeric antimicrobial drugs. The vancomycin-CAPH conjugate, VanP14S, showed enhanced mammalian cell uptake compared to vancomycin, a poor mammalian cell-penetrating agent; and VanP14S was capable of cleaving and releasing two antibiotics under mimicked physiological conditions. Enhanced antibacterial activity was observed against a spectrum of Gram-positive and Gram-negative pathogens, including drug-resistant strains. Further investigation revealed that this conjugate’s bactericidal activity was not entirely the result of significant membrane perturbation such as a lytic mode of action. Mammalian cell toxicity and red blood cell lysis were insignificant at relevant bactericidal concentrations below 20 µM. The current results suggest an enhanced binding to the peptidoglycan of bacteria, the target of vancomycin, although more work is needed to justify this claim. Preliminary results on VanP14GAPS, a conjugate with a more rigid CAPH, convey similar activity to VanP14S; however, moderate increases in red blood cell lysis and cytotoxicity were observed.

Regarding the LnzP14 conjugate, preliminary data reveal that the conjugate has Gram-negative activity against Escherichia coli, whereas linezolid is ineffective in killing Gram-negative bacteria. This conjugate showed significant enhancement in cellular uptake compared to the CAPH, and the release of linezolid and CAPH in physiological conditions was confirmed. Overall, arming a conventional antibiotic with an antimicrobial, cell-penetrating peptide appears to be a powerful strategy in providing novel antibiotic conjugates with the propensity to overcome the limitations in treating challenging pathogens.

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Maumela, Pfariso. "The study of cationic amphiphilic peptides with anti-cancer selective toxicity." Thesis, 2014. http://hdl.handle.net/10539/15330.

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A dissertation submitted to the Faculty of Science, University of the Witwatersrand, Johannesburg, in fulfilment of the requirements for the degree of Master of Science. Johannesburg, 2014.
The exposure of organisms to environmental stresses and pathogens results in rapid activation of a range of defensive pathways that act as part of the innate immune system. The most common innate immunity response is the activation of cationic amphiphilic peptides in response to microbial infection. Moreover, cationic amphiphilic peptides possess desirable attributes for the pharmaceutical development of cancer-selective drugs. They selectively and rapidly kill cancer cells without killing normal mammalian cells and have a broad spectrum of mechanisms of action. The aim of this exploratory study was to screen for cationic amphiphilic peptides with anti-proliferative activity that is induced by genotoxicity. GeneFishing® technology, 2-D gel analysis and bioassays were used to identify and analyse molecules induced in response to genotoxic stress in an embryonic cell line originating from the dung beetle Euoniticellus intermedius. Bioassay results revealed that the cell line has constitutive expression of probable cationic amphiphilic proteins that are further induced by camptothecin treatment. GeneFishing® and 2-D gel analysis showed changes in gene expression at both transcriptional and translational levels, respectively. Overall, the study failed to identify the involvement or induction of cationic amphiphilic peptides in response to genotoxic stress. However, gene expression analyses revealed changes in the expression of classes of proteins involved in stress response, oxidative phosphorylation, mitochondrial maintenance, protein translation, cytoskeletal proteins and immunophilins. The results show that the cell line constitutively expresses probable cationic amphiphilic peptides which are further induced by camptothecin.
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Arnt, Lachelle. "Cationic facially amphiphilic phenylene ethynylenes as host defense peptide mimics." 2005. https://scholarworks.umass.edu/dissertations/AAI3179853.

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The goal of this research is to design molecules that capture the essential elements and biological properties of host defense peptides without the use of amino acids or peptide-like backbones. This is accomplished via a meta-phenylene ethynylene backbone with polar amine and nonpolar alkyl groups as side chains. These molecules are shown to form stable monolayers at the air-water interface with the polymer chains assuming an edge-on structure with the aromatic rings perpendicular to the water surface and the polar amines groups below the water surface. Furthermore, these molecules aggregate in solution with the addition of a non-solvent, as expected with facially amphiphilic molecules. When tested against biological systems, the result is promising: growth inhibition against a wide variety of bacteria at relatively low concentrations with minimal disruption towards red blood cells. The average minimal concentration needed to disrupt bacterial growth is 2 μg/mL and occurs in less than 5 minutes. Furthermore, tests indicate negligible evolution of bacterial resistance over a month-long experiment. Incorporation of these compounds into polymeric substrates proves to be an effective way of preventing bacterial growth on surfaces. Further probing the mode of action of these molecules shows results similar to many host defense peptides.
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(11014752), Ambar M. Rosario. "Synthesis of a Cationic Amphiphilic Polyproline Helix (CAPH) Conjugate with Polymyxin B." Thesis, 2021.

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Pathogens such as Listeria, Shigella, Brucella, Salmonella, Mycobacterium tuberculosis and methicillin-resistant Staphylococcus aureus (MRSA) can traverse into mammalian cells, such as phagocytic macrophages. Once inside, these bacteria can survive and reproduce, causing chronic infections. It is of utmost importance to develop novel antibiotics with broad spectrum activity to control these deadly bacteria. Broad spectrum activity will allow for targeting of pathogens with different structures and cell membrane components.
This work focuses on the synthesis of a dual antibiotic agent, composed of a cationic amphiphilic polyproline helix (CAPH) possessing cell penetrating and nonmembrane lytic antimicrobial capabilities (P14LRR), and a derivative of the polymyxin B (PMX) antibacterial peptide. This dual antibiotic conjugate was created to be a tool to potentially clear intracellular pathogenic bacteria. Overall, the reduction of the disulfide bond linking the two antibiotics within the reducing environment of cells would release the individual antimicrobial agents, and could have improved cell membrane penetration and intracellular synergistic activity. Herein, the synthesis of the dual antibiotic agent, P14LRR-PMX, is discussed.
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