Literatura académica sobre el tema "Antimicrobial peptid"
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Artículos de revistas sobre el tema "Antimicrobial peptid"
Burgettiné Böszörményi, Erzsébet, István Barcs, Gyula Domján, Katalin Bélafiné Bakó, András Fodor, László Makrai y Dávid Vozik. "A Xenorhabdus budapestensis entomopatogén baktérium sejtmentes fermentlevének és tisztítottfehérje-frakciójának antimikrobiális hatása néhány zoonoticus baktériumra". Orvosi Hetilap 156, n.º 44 (noviembre de 2015): 1782–86. http://dx.doi.org/10.1556/650.2015.30274.
Texto completoAlmsned, Fahad. "Designing Antimicrobial Peptide: Current Status". Journal of Medical Science And clinical Research 05, n.º 03 (26 de marzo de 2016): 19282–94. http://dx.doi.org/10.18535/jmscr/v5i3.153.
Texto completoBrowne, Katrina, Sudip Chakraborty, Renxun Chen, Mark DP Willcox, David StClair Black, William R. Walsh y Naresh Kumar. "A New Era of Antibiotics: The Clinical Potential of Antimicrobial Peptides". International Journal of Molecular Sciences 21, n.º 19 (24 de septiembre de 2020): 7047. http://dx.doi.org/10.3390/ijms21197047.
Texto completoArtuković Nadinić, Irena, Vladimir Mrljak, Marija Lipar, Marina Pavlak, Ljiljana Bedrica y Renata Barić Rafaj. "The peptide hormone hepcidin". Veterinarska stanica 51, n.º 2 (27 de marzo de 2020): 187–98. http://dx.doi.org/10.46419/vs.51.2.9.
Texto completoChongsiriwatana, Nathaniel P., Tyler M. Miller, Modi Wetzler, Sergei Vakulenko, Amy J. Karlsson, Sean P. Palecek, Shahriar Mobashery y Annelise E. Barron. "Short Alkylated Peptoid Mimics of Antimicrobial Lipopeptides". Antimicrobial Agents and Chemotherapy 55, n.º 1 (18 de octubre de 2010): 417–20. http://dx.doi.org/10.1128/aac.01080-10.
Texto completoHaney, Evan F., Leonard T. Nguyen, David J. Schibli y Hans J. Vogel. "Design of a novel tryptophan-rich membrane-active antimicrobial peptide from the membrane-proximal region of the HIV glycoprotein, gp41". Beilstein Journal of Organic Chemistry 8 (24 de julio de 2012): 1172–84. http://dx.doi.org/10.3762/bjoc.8.130.
Texto completoNava Lara, Rodrigo, Longendri Aguilera-Mendoza, Carlos Brizuela, Antonio Peña y Gabriel Del Rio. "Heterologous Machine Learning for the Identification of Antimicrobial Activity in Human-Targeted Drugs". Molecules 24, n.º 7 (31 de marzo de 2019): 1258. http://dx.doi.org/10.3390/molecules24071258.
Texto completoZhang, Yong-lian y Hsiao-Chang Chan. "S1h1-4 An epididymis-specific antimicrobial peptide has dual functions in sperm maturation(S1-h1 "Antimicrobial Peptides and Membrane Interactions",Symposia,Abstract,Meeting Program of EABS & BSJ 2006)". Seibutsu Butsuri 46, supplement2 (2006): S113. http://dx.doi.org/10.2142/biophys.46.s113_2.
Texto completoSutyak Noll, Katia, Mark N. Prichard, Arkady Khaykin, Patrick J. Sinko y Michael L. Chikindas. "The Natural Antimicrobial Peptide Subtilosin Acts Synergistically with Glycerol Monolaurate, Lauric Arginate, and ε-Poly-l-Lysine against Bacterial Vaginosis-Associated Pathogens but Not Human Lactobacilli". Antimicrobial Agents and Chemotherapy 56, n.º 4 (17 de enero de 2012): 1756–61. http://dx.doi.org/10.1128/aac.05861-11.
Texto completoС., Саха, Ратрей П. y Мишра А. "ВЗАИМОДЕЙСТВИЕ АНТИМИКРОБНОГО ПЕПТИДА ЛАЗИОГЛОССИНА III С МОДЕЛЬНЫМИ ЛИПИДНЫМИ БИСЛОЯМИ". Биофизика 67, n.º 2 (2022): 250–63. http://dx.doi.org/10.31857/s0006302922020077.
Texto completoTesis sobre el tema "Antimicrobial peptid"
Dannehl, Claudia. "Fragments of the human antimicrobial LL-37 and their interaction with model membranes". Phd thesis, Universität Potsdam, 2013. http://opus.kobv.de/ubp/volltexte/2013/6814/.
Texto completoAufgrund der steigenden Resistenzen von Zellstämmen gegen traditionelle Therapeutika sind alternative medizinische Behandlungsmöglichkeiten für bakterielle Infektionen und Krebs stark gefragt. Antimikrobielle Peptide (AMPs) sind Bestandteil der unspezifischen Immunabwehr und kommen in jedem Organismus vor. AMPs lagern sich von außen an die Zellmembran an und zerstören ihre Integrität. Das macht sie effizient und vor allem schnell in der Wirkung gegen Bakterien, Viren, Pilzen und sogar Krebszellen. Das Ziel dieser Arbeit lag in der physikalisch-chemischen Charakterisierung zweier Peptidfragmente die unterschiedliche biologische Aktivität aufweisen. Die Peptide LL-32 und LL-20 waren Teile des humanen LL-37 aus der Kathelizidin-Familie. LL-32 wies eine stärke Aktivität als das Mutterpeptid auf, während LL-20 kaum aktiv gegen die verschiedenen Zelltypen war. In dieser Arbeit wurde die Wechselwirkung der Peptide mit Zellmembranen systematisch anhand von zweidimensionalen Modellmembranen in dieser Arbeit untersucht. Dafür wurden Filmwaagenmessungen mit IR-spektroskopischen und Röntgenstreumethoden gekoppelt. Circulardichroismus-Spektroskopie im Volumen komplementierte die Ergebnisse. In der ersten Näherung wurde die Struktur der Peptide in Lösung mit der Struktur an der Wasser/Luft-Grenzfläche verglichen. In wässriger Lösung sind beide Peptidfragmente unstrukturiert, nehmen jedoch eine α-helikale Sekundärstruktur an, wenn sie an die Wasser/Luft-Grenzfläche adsorbiert sind. Das biologisch unwirksamere LL-20 bleibt dabei teilweise ungeordnet. Das steht im Zusammenhang mit einer geringeren Grenzflächenaktivität des Peptids. In der Zweiten Näherung wurden Versuche mit Lipidmonoschichten als biomimetisches Modell für die Wechselwirkung mit der Zellmembran durchgeführt. Es konnte gezeigt werden, dass sich die Peptide fluidisierend auf negativ geladene Dipalmitylphosphatidylglycerol (DPPG) Monoschichten auswirken, was einer Membranverdünnung an Bakterienzellen entspricht. Eine Interaktion der Peptide mit zwitterionischem Phosphatidylcholin (PC), das als Modell für Säugetierzellen verwendet wurde, konnte nicht klar beobachtet werden, obwohl biologische Experimente das hämolytische Verhalten zumindest von LL-32 zeigten. In der dritten Näherung wurde das Membranmodell näher an die Membran von humanen Erythrozyten angepasst, indem gemischte Monoschichten aus Sphingomyelin (SM) und PC hergestellt wurden. Die physikalisch-chemischen Eigenschaften der Lipidfilme wurden zunächst ausgearbeitet und anschließend der Einfluss der Peptide untersucht. Es konnte anhand verschiedener Versuche gezeigt werden, dass die Wechselwirkung von LL-32 mit der Modellmembran verstärkt ist, wenn eine Koexistenz von fluiden und Gelphasen auftritt. Zusätzlich wurde die Wechselwirkung der Peptide mit der Membran von Krebszellen imitiert, indem ein geringer Anteil negativ geladener Lipide in die Monoschicht eingebaut wurde. Das hatte allerdings keinen nachweislichen Effekt, so dass geschlussfolgert werden konnte, dass die hohe Aktivität von LL-32 gegen Krebszellen ihren Grund in der veränderten Fluidität der Membran hat und nicht in der veränderten Oberflächenladung. Darüber hinaus wurden Ähnlichkeiten zu Melittin, einem AMP aus dem Bienengift, dargelegt. Die Ergebnisse dieser Arbeit sprechen für einen Detergenzien-artigen Wirkmechanismus des Peptids LL-32 an der Zellmembran.
Das, Sanjit. "Methodological development in peptide chemistry for synthesis of antimicrobial and antifungal derivatives of marine natural peptides". Thesis, Perpignan, 2018. http://www.theses.fr/2018PERP0054.
Texto completoThe click chemistry has become indispensible in the many areas of chemistry associated with drug design. In this context, as we know the study concerning the impact of triazole insertion on the conformation of peptaibol is limited, we have conducted the study to investigate the impact and adaptability of the 1, 4-disubstituted 1, 2, 3-triazole insertion into different peptaibols. Depending on the outcome of this experiment relating to reduced activity and perturbed conformation of the peptaibol analogue, the dipeptide surrogate decorated with the triazole moiety bearing various hydrophobic substituents was inserted at the very N-ter part of the peptaibol. The improvement of the bioactivity and restoration of the conformation for the peptaibol analogues was observed and the fact was also supported by the results obtained from the biophysical study of the selected analogues of ALM F50/5. We have further extended our study to employ our strategy to be applied on the therapeutic P42 peptide which suffers from the limitation of lack of permeability and stability. P42 peptide is involved in the pathophysiology of neurodegenerative Huntington’s disease. A total of 12 analogues of P42-TAT peptide were synthesized through SPPS by our optimized protocol. In the second part, we have developed a strategy for synthesizing the cyclic lipopeptide originated from marine cynaobacterial species. Our main objective was to synthesize Hormothamnin A, a cyclic undecapeptide consisting of several unnatural amino acids including dehydroamino acid (Dhaa) which makes the synthesis of this peptide complicated. Due to this reason, firstly, we have chosen to apply our strategy to synthesize Trichormamide A, a relatively simpler kind of cylic lipopeptide. After accomplishing this task, a first attempt was made to synthesize Hormothamnin A. The preliminary result of this is presented in this section. At last, we have tried to develop a robust methodology to synthesize Fmoc-Dhaa in solution phase and its insertion into the peptaibol sequence through a standard SPPS protocol. The preliminary results we have got concerning the Dhaa synthesis and its insertion into peptaibol are also discussed here in addition with the solid phase synthesis of natural Bergofungin D
Weichbrodt, Conrad. "Elektrophysiologische Charakterisierung des mitochondrialen Porins VDAC1 und des antimikrobiellen Peptids Dermcidin in lösungsmittelfreien Modellmembranen". Doctoral thesis, Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2013. http://hdl.handle.net/11858/00-1735-0000-0001-BAA4-C.
Texto completoShyam, Radhe. "Cationic amphipathic peptoid oligomers as antimicrobial peptide mimics". Thesis, Université Clermont Auvergne (2017-2020), 2018. http://www.theses.fr/2018CLFAC048/document.
Texto completoLiving 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
Rolland, Jean-Luc. "Aspects moléculaires et biochimiques des stylicines, peptides multifonctionnels identifiés chez la crevette bleue du Pacifique Litopenaeus stylirostris (Crustacea, Decapoda)". Thesis, Montpellier 2, 2010. http://www.theses.fr/2010MON20049.
Texto completoThe work reported here was motivated by the economical importance of the pacific blue shrimp Litopenaeus stylirostris farming where high mortality rates are due to bacterial and viral diseases. It consists in the characterisation of two original peptides, the first members of a new multifunctional family of peptides from peneide shrimps, the stylicines. Those two peptides, named stylicines 1 and 2, are negatively charged (pI < 6.0), and characterised by a proline-rich N-terminal region and a C-terminal region containing 13 cysteine residues. Stylicines are synthesized by heamocytes where they are stored within small cytoplasmic granules. To understand the role of these peptides in the immune response of shrimps to a vibrio infection, their recombinant forms were produced in E. coli BL21 (DE3) plysS, purified and characterised. The two rstylicines display biological anti-proliferative and blood clotting activities. Only rstylicine 1 displays antimicrobial activities: antifungal against Fusarium oxysporum (MIC<2.5µM) and bacteriostatic against Gram (−) bacteria, Vibrio sp. (MIC<80µM). Moreover this peptide displays an LPS-binding activity (dissociation constant (Kd) of 9.6×10−8 M) and agglutinate Vibrio. penaeicida "in vitro". Finally, the presence of sequences coding for modified forms of stylicine 1 in some shrimp's genome may be in relation with their lower ability to survive infections
FASOLI, Anna. "Biophysical mechanisms of membrane perturbation and signal transduction produced by proteins and peptides". Doctoral thesis, Università degli studi di Ferrara, 2015. http://hdl.handle.net/11392/2388995.
Texto completoZerfas, Breanna L. "Creating Novel Antimicrobial Peptides: From Gramicidin A to Screening a Cyclic Peptide Library". Thesis, Boston College, 2017. http://hdl.handle.net/2345/bc-ir:107444.
Texto completoAs the threat of microbial resistance to antibiotics grows, we must turn in new directions to find new drugs effective against resistant infections. Antimicrobial peptides (AMPs) and host-defense peptides (HDPs) are a class of natural products that have been well-studied towards this goal, though very few have found success clinically. However, as there is much known about the behavior of these peptides, work has been done to manipulate their sequences and structures in the search for more drug-like properties. Additionally, novel sequences and structures mimicking those seen in nature have been discovered and characterized. Herein, we demonstrate our ability to finely tune the antimicrobial activity of various peptides, such that they can be provided with more clinically desirable characteristics. Our results show that gramicidin A (gA) can be made to be less toxic via incorporation of unnatural cationic amino acids. This is achieved by synthesizing lysine analogues with diverse hydrophobic groups alkylated to the side-chain amine. Through exploring different groups, we achieved peptide structures with improved selectivity for bacterial over mammalian membranes. Additionally, we were able to achieve novel broad-spectrum gram-negative activity for gA peptides. In efforts to combat bacterial resistance to cationic antimicrobial peptides (CAMPs), we have directed our reported amine-targeting iminoboronate chemistry towards neutralizing Lys-PG in bacterial membranes. Originally incorporating 2-APBA into gA, we found this to hinder the peptide’s activity. However, we were successful in increasing the potency of gA3R, a cationic mutant of gA, towards S. aureus by using a co-treatment of this peptide with a Lys-PG binding structure. Currently, we are exploring this strategy further. Finally, we describe our work towards establishing a novel cyclic peptide library incorporating a 2-APBA warhead for iminoboronate formation with a given target. In this, we have achieved intermolecular reduction of iminoboronates, strengthening the stringency of library screening. Although we were unsuccessful in finding a potent hit for binding of the lipid II stem peptide, screening against human transferrin yielded selective hits. Currently we are investigating these hits to understand their activity and therapeutic potential
Thesis (PhD) — Boston College, 2017
Submitted to: Boston College. Graduate School of Arts and Sciences
Discipline: Chemistry
Borrelli, Alexander P. "Synthetic Genes for Antimicrobial Peptides". Digital WPI, 2003. https://digitalcommons.wpi.edu/etd-theses/427.
Texto completoJodoin, Joelle. "Histone H5: Bioinspiration for Novel Antimicrobial Peptides". Thesis, Université d'Ottawa / University of Ottawa, 2017. http://hdl.handle.net/10393/36976.
Texto completoLinser, Sebastian. "Development of new antimicrobial peptides based on the synthetic peptide NK-2". [S.l.] : [s.n.], 2006. http://deposit.ddb.de/cgi-bin/dokserv?idn=982021631.
Texto completoLibros sobre el tema "Antimicrobial peptid"
Joan, Marsh, Goode Jamie, Ciba Foundation y Symposium on Antimicrobial Peptides (1994 : Ciba Foundation)d), eds. Antimicrobial peptides. Chichester, Eng: Wiley, 1994.
Buscar texto completoHansen, Paul R., ed. Antimicrobial Peptides. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6737-7.
Texto completoMatsuzaki, Katsumi, ed. Antimicrobial Peptides. Singapore: Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-13-3588-4.
Texto completoPhoenix, David A., Sarah R. Dennison y Frederick Harris. Antimicrobial Peptides. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527652853.
Texto completoGiuliani, Andrea y Andrea C. Rinaldi, eds. Antimicrobial Peptides. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-594-1.
Texto completoHarder, Jürgen y Jens-M. Schröder, eds. Antimicrobial Peptides. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-24199-9.
Texto completoAntimicrobial peptides: Methods and protocols. New York: Humana Press/Springer, 2010.
Buscar texto completoDrider, Djamel y Sylvie Rebuffat, eds. Prokaryotic Antimicrobial Peptides. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-7692-5.
Texto completoL, Gallo Richard, ed. Antimicrobial peptides in human health and disease. Wymondham, U.K: Horizon Bioscience, 2005.
Buscar texto completoDrider, Djamel y Sylvie Rebuffat. Prokaryotic antimicrobial peptides: From genes to applications. New York: Springer Verlag, 2011.
Buscar texto completoCapítulos de libros sobre el tema "Antimicrobial peptid"
Bryskier, A. "Peptide Antibiotics". En Antimicrobial Agents, 826–79. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555815929.ch30.
Texto completoMarcos, Jose F. y Paloma Manzanares. "Antimicrobial Peptides". En Antimicrobial Polymers, 195–225. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9781118150887.ch8.
Texto completoPark, Andrew J., Jean-Phillip Okhovat y Jenny Kim. "Antimicrobial Peptides". En Clinical and Basic Immunodermatology, 81–95. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-29785-9_6.
Texto completoChakraborti, Srinjoy y Sanjay Ram. "Antimicrobial Peptides". En Management of Infections in the Immunocompromised Host, 95–113. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-77674-3_5.
Texto completoJack, Ralph W., Gabriele Bierbaum y Hans-Georg Sahl. "Antimicrobial Peptides". En Lantibiotics and Related Peptides, 1–39. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-662-08239-3_1.
Texto completoLata, Sneh y Gajendra Raghava. "Antimicrobial Peptides". En Encyclopedia of Systems Biology, 31–33. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-9863-7_87.
Texto completoGanz, T. y R. I. Lehrer. "Antimicrobial Peptides". En Handbook of Experimental Pharmacology, 295–304. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-642-55742-2_16.
Texto completoSørensen, Ole E. "Antimicrobial Peptides in Cutaneous Wound Healing". En Antimicrobial Peptides, 1–15. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24199-9_1.
Texto completoZasloff, Michael. "Antimicrobial Peptides: Do They Have a Future as Therapeutics?" En Antimicrobial Peptides, 147–54. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24199-9_10.
Texto completoGarreis, Fabian, Martin Schicht y Friedrich Paulsen. "Antimicrobial Peptides as Endogenous Antibacterials and Antivirals at the Ocular Surface". En Antimicrobial Peptides, 17–32. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24199-9_2.
Texto completoActas de conferencias sobre el tema "Antimicrobial peptid"
Reinoso, Zain Sanchez, Jacinthe Thibodeau, Laila Ben Said, Ismail Fliss, Laurent Bazinet y Sergey Mikhaylin. "Bioactive Peptide Production from Slaughterhouse Blood Proteins: Impact of Pulsed Electric Fields and Ph on Enzyme Inactivation, Antimicrobial and Antioxidant Activities of Peptic Hydrolysates from Bovine and Porcine Hemoglobins". En 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/fsht2150.
Texto completoSoares, Jason W. y Charlene M. Mello. "Antimicrobial peptides: a review of how peptide structure impacts antimicrobial activity". En Optical Technologies for Industrial, Environmental, and Biological Sensing, editado por Bent S. Bennedsen, Yud-Ren Chen, George E. Meyer, Andre G. Senecal y Shu-I. Tu. SPIE, 2004. http://dx.doi.org/10.1117/12.516171.
Texto completoConnolly, John R. F. B., Deirdre Fitzgerald-Hughes y Marc Devocelle. "Novel Antimicrobial Peptide Fluoroquinolone Conjugates". En 36th European Peptide Symposium. The European Peptide Society, 2022. http://dx.doi.org/10.17952/36eps/36eps.2022.062.
Texto completoMałuch, Izabela, Oktawian Stachurski, Paulina Kosikowska-Adamus, Dariusz Wyrzykowski, Adam Prahl y Emilia Sikorska. "Double-head lipopeptide surfactants as potential antimicrobial agents". En 35th European Peptide Symposium. Prompt Scientific Publishing, 2018. http://dx.doi.org/10.17952/35eps.2018.153.
Texto completoOlkiewicz, Katarzyna, Anna Łegowska, Natalia Ptaszynska, Agata Gitlin-Domagalska, Dawid Debowski, Joanna Okonska, Dorota Martynow, Marcin Serocki, Sławomir Milewski y Krzysztof Rolka. "Peptide conjugates of transportan10 with antimicrobial and antifungal antibiotics". En 35th European Peptide Symposium. Prompt Scientific Publishing, 2018. http://dx.doi.org/10.17952/35eps.2018.309.
Texto completoCantallops-Vilà, Cristina, Laura Colomina-Alfaro, Pietro Riccio, Hanieh Ijakipour, Edwige Meurice, Antonella Bandiera y Artemis Stamboulis. "Different Strategies of Antimicrobial Peptides Production for Biomedical Applications". En 36th European Peptide Symposium. The European Peptide Society, 2022. http://dx.doi.org/10.17952/36eps/36eps.2022.039.
Texto completoGarg, Tripti, George Konstantinidis, Joan Peckham, Admir Monteiro, Roxanne LaCroix y Lenore M. Martin. "Designing AMPed: The Practical Antimicrobial Peptide Editable Database". En The 24th American Peptide Symposium. Prompt Scientific Publishing, 2015. http://dx.doi.org/10.17952/24aps.2015.105.
Texto completoTuránek, Jaroslav, Michaela Škrabalová y Pavlína Knötigová. "Antimicrobial and anticancer peptides". En XIth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2009. http://dx.doi.org/10.1135/css200911128.
Texto completoPlisson, Fabien. "Overcoming the Challenges in Machine Learning-Guided Antimicrobial Peptide Design". En 36th European Peptide Symposium. The European Peptide Society, 2022. http://dx.doi.org/10.17952/36eps/36eps.2022.207.
Texto completoShine, Conor, Jamie MacLennan, Deirdre Fitzgerald-Hughes y Marc Devocelle. "New Generation of Polyethylene Glycol (PEG)-Based Peptidomimetics of Antimicrobial Peptides (AMPs)". En 36th European Peptide Symposium. The European Peptide Society, 2022. http://dx.doi.org/10.17952/36eps/36eps.2022.086.
Texto completoInformes sobre el tema "Antimicrobial peptid"
Vouros, Paul y Terrance Black. Solid Phase Peptide Synthesis of Antimicrobial Peptides for cell Binding Studies: Characterization Using Mass Spectrometry. Fort Belvoir, VA: Defense Technical Information Center, noviembre de 2002. http://dx.doi.org/10.21236/ada412571.
Texto completoDoherty, Laurel A., Morris Slutsky y Jason W. Soares. Antimicrobial Peptides with Differential Bacterial Binding Characteristics. Fort Belvoir, VA: Defense Technical Information Center, marzo de 2013. http://dx.doi.org/10.21236/ada577726.
Texto completoMierswa, S. C., T. H. Lee y M. C. Yung. Developing an engineered therapeutic microbe to release antimicrobial peptides (AMPs). Office of Scientific and Technical Information (OSTI), agosto de 2019. http://dx.doi.org/10.2172/1558856.
Texto completoYung, M. C. Engineering a therapeutic microbe for site-of-infection delivery of encapsulated antimicrobial peptides (AMPs). Office of Scientific and Technical Information (OSTI), octubre de 2019. http://dx.doi.org/10.2172/1573149.
Texto completoNoga, Edward J., Angelo Colorni, Michael G. Levy y Ramy Avtalion. Importance of Endobiotics in Defense against Protozoan Ectoparasites of Fish. United States Department of Agriculture, septiembre de 2003. http://dx.doi.org/10.32747/2003.7586463.bard.
Texto completoReisch, Bruce, Avichai Perl, Julie Kikkert, Ruth Ben-Arie y Rachel Gollop. Use of Anti-Fungal Gene Synergisms for Improved Foliar and Fruit Disease Tolerance in Transgenic Grapes. United States Department of Agriculture, agosto de 2002. http://dx.doi.org/10.32747/2002.7575292.bard.
Texto completoDroby, Samir, Michael Wisniewski, Martin Goldway, Wojciech Janisiewicz y Charles Wilson. Enhancement of Postharvest Biocontrol Activity of the Yeast Candida oleophila by Overexpression of Lytic Enzymes. United States Department of Agriculture, noviembre de 2003. http://dx.doi.org/10.32747/2003.7586481.bard.
Texto completoCytryn, Eddie, Mark R. Liles y Omer Frenkel. Mining multidrug-resistant desert soil bacteria for biocontrol activity and biologically-active compounds. United States Department of Agriculture, enero de 2014. http://dx.doi.org/10.32747/2014.7598174.bard.
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