Статті в журналах з теми "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.
Повний текст джерелаAkkarawongsa, Radeekorn, Terra B. Potocky, Emily P. English, Samuel H. Gellman та Curtis R. Brandt. "Inhibition of Herpes Simplex Virus Type 1 Infection by Cationic β-Peptides". Antimicrobial Agents and Chemotherapy 52, № 6 (7 квітня 2008): 2120–29. http://dx.doi.org/10.1128/aac.01424-07.
Повний текст джерелаSchweizer, 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.
Повний текст джерелаFindlay, 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.
Повний текст джерелаKaconis, 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.
Повний текст джерелаCao, 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.
Повний текст джерелаWiradharma, Nikken, Ulung Khoe, Charlotte A. E. Hauser, See Voon Seow, Shuguang Zhang та Yi-Yan Yang. "Synthetic cationic amphiphilic α-helical peptides as antimicrobial agents". Biomaterials 32, № 8 (березень 2011): 2204–12. http://dx.doi.org/10.1016/j.biomaterials.2010.11.054.
Повний текст джерелаKundu, 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.
Повний текст джерелаRideout, 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.
Повний текст джерелаStrandberg, 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 (1 січня 2007): 717–28. http://dx.doi.org/10.1351/pac200779040717.
Повний текст джерелаAmirkhanov, 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 (September 2018): 492–503. http://dx.doi.org/10.1134/s1068162018050035.
Повний текст джерелаXiong, Menghua, Michelle W. Lee, Rachael A. Mansbach, Ziyuan Song, Yan Bao, Richard M. Peek, Catherine Yao, et al. "Helical antimicrobial polypeptides with radial amphiphilicity." Proceedings of the National Academy of Sciences 112, no. 43 (October 12, 2015): 13155–60. http://dx.doi.org/10.1073/pnas.1507893112.
Повний текст джерелаHwang, Peter M., and Hans J. Vogel. "Structure-function relationships of antimicrobial peptides." Biochemistry and Cell Biology 76, no. 2-3 (May 1, 1998): 235–46. http://dx.doi.org/10.1139/o98-026.
Повний текст джерелаFuchigami, Takeshi, Takeshi Chiga, Sakura Yoshida, Makoto Oba, Yu Fukushima, Hiromi Inoue, Akari Matsuura, Akira Toriba, and Morio Nakayama. "Synthesis and Characterization of Radiogallium-Labeled Cationic Amphiphilic Peptides as Tumor Imaging Agents." Cancers 13, no. 10 (May 14, 2021): 2388. http://dx.doi.org/10.3390/cancers13102388.
Повний текст джерелаHuo, Yehong, Linhao Ma, Mengzhi Zhang, Mingcong Niu, Xiulian Gu, Wenjie Zhang, Miaomiao Yan, and Guangcheng Wei. "Development of anticancer peptides with low hemolysis, high penetrating membrane activity, certain analgesic activity and the synergistic anticancer effect." Biomaterials Science 10, no. 7 (2022): 1724–41. http://dx.doi.org/10.1039/d1bm02024b.
Повний текст джерелаWang, Hao, Mingcong Niu, Tong Xue, Linhao Ma, Xiulian Gu, Guangcheng Wei, Fengqiao Li, and Chunhua Wang. "Development of antibacterial peptides with efficient antibacterial activity, low toxicity, high membrane disruptive activity and a synergistic antibacterial effect." Journal of Materials Chemistry B 10, no. 11 (2022): 1858–74. http://dx.doi.org/10.1039/d1tb02852a.
Повний текст джерелаYosefi, Gal, Ifat Cohen‐Erez, Einat Nativ‐Roth, Hanna Rapaport та Ronit Bitton. "Spontaneous Alignment of Self‐Assembled Cationic and Amphiphilic β‐Sheet Peptides". Advanced Materials Interfaces 7, № 14 (22 червня 2020): 2000332. http://dx.doi.org/10.1002/admi.202000332.
Повний текст джерелаMandal, Santi M., and Souvik Panda. "Inhaler with electrostatic sterilizer and use of cationic amphiphilic peptides may accelerate recovery from COVID-19." BioTechniques 69, no. 3 (September 2020): 206–10. http://dx.doi.org/10.2144/btn-2020-0042.
Повний текст джерелаDiaferia, Carlo, Elisabetta Rosa, Enrico Gallo, Giovanni Smaldone, Mariano Stornaiuolo, Giancarlo Morelli, and Antonella Accardo. "Self-Supporting Hydrogels Based on Fmoc-Derivatized Cationic Hexapeptides for Potential Biomedical Applications." Biomedicines 9, no. 6 (June 15, 2021): 678. http://dx.doi.org/10.3390/biomedicines9060678.
Повний текст джерелаHadianamrei, Roja, Jiqian Wang, Stephen Brown, and Xiubo Zhao. "Rationally designed cationic amphiphilic peptides for selective gene delivery to cancer cells." International Journal of Pharmaceutics 617 (April 2022): 121619. http://dx.doi.org/10.1016/j.ijpharm.2022.121619.
Повний текст джерелаMosca, Simone, Janos Keller, Nahid Azzouz, Stefanie Wagner, Alexander Titz, Peter H. Seeberger, Gerald Brezesinski та Laura Hartmann. "Amphiphilic Cationic β3R3-Peptides: Membrane Active Peptidomimetics and Their Potential as Antimicrobial Agents". Biomacromolecules 15, № 5 (15 квітня 2014): 1687–95. http://dx.doi.org/10.1021/bm500101w.
Повний текст джерелаDamen, Mark, Mario Izidoro, Debora Okamoto, Lilian Oliveira, Helene Amatdjais-Groenen, Stijn van Dongen, Koen van Cleef, et al. "Cationic Geminoid Peptide Amphiphiles Inhibit DENV2 Protease, Furin, and Viral Replication." Molecules 27, no. 10 (May 17, 2022): 3217. http://dx.doi.org/10.3390/molecules27103217.
Повний текст джерелаBultmann, Hermann, Gary Girdaukas, Glen S. Kwon, and Curtis R. Brandt. "The Virucidal EB Peptide Protects Host Cells from Herpes Simplex Virus Type 1 Infection in the Presence of Serum Albumin and Aggregates Proteins in a Detergent-Like Manner." Antimicrobial Agents and Chemotherapy 54, no. 10 (July 19, 2010): 4275–89. http://dx.doi.org/10.1128/aac.00495-10.
Повний текст джерелаHartmann, Mareike, Marina Berditsch, Jacques Hawecker, Mohammad Fotouhi Ardakani, Dagmar Gerthsen, and Anne S. Ulrich. "Damage of the Bacterial Cell Envelope by Antimicrobial Peptides Gramicidin S and PGLa as Revealed by Transmission and Scanning Electron Microscopy." Antimicrobial Agents and Chemotherapy 54, no. 8 (June 7, 2010): 3132–42. http://dx.doi.org/10.1128/aac.00124-10.
Повний текст джерелаPark, Jung Woo, Eun-Kyoung Bang, Eun Mi Jeon, and Byeang Hyean Kim. "Complexation and conjugation approaches to evaluate siRNA delivery using cationic, hydrophobic and amphiphilic peptides." Org. Biomol. Chem. 10, no. 1 (2012): 96–102. http://dx.doi.org/10.1039/c1ob06042b.
Повний текст джерелаHuang, Yuan, Nikken Wiradharma, Kaijin Xu, Zhongkang Ji, Sheng Bi, Lanjuan Li, Yi-Yan Yang, and Weimin Fan. "Cationic amphiphilic alpha-helical peptides for the treatment of carbapenem-resistant Acinetobacter baumannii infection." Biomaterials 33, no. 34 (December 2012): 8841–47. http://dx.doi.org/10.1016/j.biomaterials.2012.08.026.
Повний текст джерелаRyder, Matthew P., Xiangming Wu, Greg R. McKelvey, Joseph McGuire, and Karl F. Schilke. "Binding interactions of bacterial lipopolysaccharide and the cationic amphiphilic peptides polymyxin B and WLBU2." Colloids and Surfaces B: Biointerfaces 120 (August 2014): 81–87. http://dx.doi.org/10.1016/j.colsurfb.2014.05.004.
Повний текст джерелаDubovskii, P. V., and Y. N. Utkin. "Cobra Cytotoxins: Structural Organization and Antibacterial Activity." Acta Naturae 6, no. 3 (September 15, 2014): 11–18. http://dx.doi.org/10.32607/20758251-2014-6-3-11-18.
Повний текст джерелаSepahi, Mina, Reza Ahangari Cohan, Shahin Hadadian, and Dariush Norouzian. "Effect of glutamic acid elimination/substitution on the biological activities of S3 cationic amphiphilic peptides." Preparative Biochemistry & Biotechnology 50, no. 7 (June 8, 2020): 664–72. http://dx.doi.org/10.1080/10826068.2020.1725772.
Повний текст джерелаLi, Yue-Xuan, Yushuang Wei, and Hong-Bo Pang. "Abstract 369: Improving the nanomaterial delivery by using cell-penetrating peptides in the bystander manner." Cancer Research 82, no. 12_Supplement (June 15, 2022): 369. http://dx.doi.org/10.1158/1538-7445.am2022-369.
Повний текст джерелаMousli, Mouaiak, Jean-Luc Bueb, Christian Bronner, Bruno Rouot, and Yves Landry. "G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides." Trends in Pharmacological Sciences 11, no. 9 (September 1990): 358–62. http://dx.doi.org/10.1016/0165-6147(90)90179-c.
Повний текст джерелаBarba-Bon, Andrea, Giulia Salluce, Irene Lostalé-Seijo, Khaleel I. Assaf, Andreas Hennig, Javier Montenegro, and Werner M. Nau. "Boron clusters as broadband membrane carriers." Nature 603, no. 7902 (March 23, 2022): 637–42. http://dx.doi.org/10.1038/s41586-022-04413-w.
Повний текст джерелаLi, Yue-Xuan, Yushuang Wei, Rui Zhong, Ling Li, and Hong-Bo Pang. "Transportan Peptide Stimulates the Nanomaterial Internalization into Mammalian Cells in the Bystander Manner through Macropinocytosis." Pharmaceutics 13, no. 4 (April 14, 2021): 552. http://dx.doi.org/10.3390/pharmaceutics13040552.
Повний текст джерелаBrunner, Sascha R., Joseph F. A. Varga, and Brian Dixon. "Antimicrobial Peptides of Salmonid Fish: From Form to Function." Biology 9, no. 8 (August 18, 2020): 233. http://dx.doi.org/10.3390/biology9080233.
Повний текст джерелаManoharan, Manovina, and Thamarai Selvi Balasubramaniam. "An Extensive Review on Production, Purification, and Bioactive Application of Different Classes of Bacteriocin." Journal of Tropical Biodiversity and Biotechnology 7, no. 3 (September 9, 2022): 72735. http://dx.doi.org/10.22146/jtbb.72735.
Повний текст джерелаWang, Chenxuan, Naomi A. Biok, Karthik Nayani, Xiaoguang Wang, Hongseung Yeon, Chi-Kuen Derek Ma, Samuel H. Gellman та Nicholas L. Abbott. "Cationic Side Chain Identity Directs the Hydrophobically Driven Self-Assembly of Amphiphilic β-Peptides in Aqueous Solution". Langmuir 37, № 11 (8 березня 2021): 3288–98. http://dx.doi.org/10.1021/acs.langmuir.0c03255.
Повний текст джерелаReijmar, Karin, Katarina Edwards, Karl Andersson, and Víctor Agmo Hernández. "Characterizing and Controlling the Loading and Release of Cationic Amphiphilic Peptides onto and from PEG-Stabilized Lipodisks." Langmuir 32, no. 46 (November 7, 2016): 12091–99. http://dx.doi.org/10.1021/acs.langmuir.6b03012.
Повний текст джерелаRuczyński, Jarosław, Brygida Parfianowicz, Piotr Mucha, Katarzyna Wiśniewska, Lidia Piechowicz, and Piotr Rekowski. "Structure–Activity Relationship of New Chimeric Analogs of Mastoparan from the Wasp Venom Paravespula lewisii." International Journal of Molecular Sciences 23, no. 15 (July 27, 2022): 8269. http://dx.doi.org/10.3390/ijms23158269.
Повний текст джерелаLocock, Katherine E. S., Thomas D. Michl, Hans J. Griesser, Matthias Haeussler, and Laurence Meagher. "Structure–activity relationships of guanylated antimicrobial polymethacrylates." Pure and Applied Chemistry 86, no. 8 (August 20, 2014): 1281–91. http://dx.doi.org/10.1515/pac-2014-0213.
Повний текст джерелаErgene, Cansu, and Edmund F. Palermo. "Antimicrobial Synthetic Polymers: An Update on Structure-Activity Relationships." Current Pharmaceutical Design 24, no. 8 (May 14, 2018): 855–65. http://dx.doi.org/10.2174/1381612824666180213140732.
Повний текст джерелаIwata, Takahiro, Hisaaki Hirose, Kentarou Sakamoto, Yusuke Hirai, Jan Vincent V. Arafiles, Misao Akishiba, Miki Imanishi, and Shiroh Futaki. "Liquid Droplet Formation and Facile Cytosolic Translocation of IgG in the Presence of Attenuated Cationic Amphiphilic Lytic Peptides." Angewandte Chemie 133, no. 36 (July 8, 2021): 19957–65. http://dx.doi.org/10.1002/ange.202105527.
Повний текст джерелаIwata, Takahiro, Hisaaki Hirose, Kentarou Sakamoto, Yusuke Hirai, Jan Vincent V. Arafiles, Misao Akishiba, Miki Imanishi, and Shiroh Futaki. "Liquid Droplet Formation and Facile Cytosolic Translocation of IgG in the Presence of Attenuated Cationic Amphiphilic Lytic Peptides." Angewandte Chemie International Edition 60, no. 36 (July 9, 2021): 19804–12. http://dx.doi.org/10.1002/anie.202105527.
Повний текст джерелаMurata, Masayuki, Sho Takahashi, Satoshi Kagiwada, Atsushi Suzuki, and Shunichi Ohnishi. "pH-Dependent membrane fusion and vesiculation of phospholipid large unilamellar vesicles induced by amphiphilic anionic and cationic peptides." Biochemistry 31, no. 7 (February 1992): 1986–92. http://dx.doi.org/10.1021/bi00122a013.
Повний текст джерелаRiahifard, Neda, Saghar Mozaffari, Taibah Aldakhil, Francisco Nunez, Qamar Alshammari, Saud Alshammari, Jason Yamaki, Keykavous Parang, and Rakesh Tiwari. "Design, Synthesis, and Evaluation of Amphiphilic Cyclic and Linear Peptides Composed of Hydrophobic and Positively-Charged Amino Acids as Antibacterial Agents." Molecules 23, no. 10 (October 22, 2018): 2722. http://dx.doi.org/10.3390/molecules23102722.
Повний текст джерелаYu, Tsz Tin, Rajesh Kuppusamy, Muhammad Yasir, Md Musfizur Hassan, Manjulatha Sara, Junming Ho, Mark D. P. Willcox, David StC Black, and Naresh Kumar. "Polyphenylglyoxamide-Based Amphiphilic Small Molecular Peptidomimetics as Antibacterial Agents with Anti-Biofilm Activity." International Journal of Molecular Sciences 22, no. 14 (July 8, 2021): 7344. http://dx.doi.org/10.3390/ijms22147344.
Повний текст джерелаHadianamrei, Roja, Mhd Anas Tomeh, Stephen Brown, Jiqian Wang та Xiubo Zhao. "Correlation between the secondary structure and surface activity of β-sheet forming cationic amphiphilic peptides and their anticancer activity". Colloids and Surfaces B: Biointerfaces 209 (січень 2022): 112165. http://dx.doi.org/10.1016/j.colsurfb.2021.112165.
Повний текст джерелаTisch, D., Y. Sharoni, M. Danilenko, and I. Aviram. "The assembly of neutrophil NADPH oxidase: effects of mastoparan and its synthetic analogues." Biochemical Journal 310, no. 2 (September 1, 1995): 715–19. http://dx.doi.org/10.1042/bj3100715.
Повний текст джерелаBalachandran, Chandrasekar, Kenta Yokoi, Kana Naito, Jebiti Haribabu, Yuichi Tamura, Masakazu Umezawa, Koji Tsuchiya, Toshitada Yoshihara, Seiji Tobita, and Shin Aoki. "Cyclometalated Iridium(III) Complex–Cationic Peptide Hybrids Trigger Paraptosis in Cancer Cells via an Intracellular Ca2+ Overload from the Endoplasmic Reticulum and a Decrease in Mitochondrial Membrane Potential." Molecules 26, no. 22 (November 21, 2021): 7028. http://dx.doi.org/10.3390/molecules26227028.
Повний текст джерелаKuzmenkov, Alexey I., Maria Y. Sachkova, Sergey I. Kovalchuk, Eugene V. Grishin, and Alexander A. Vassilevski. "Lachesana tarabaevi, an expert in membrane-active toxins." Biochemical Journal 473, no. 16 (August 11, 2016): 2495–506. http://dx.doi.org/10.1042/bcj20160436.
Повний текст джерелаRAJ, Periathamby Antony, Kavitha J. ANTONYRAJ, and Thonthi KARUNAKARAN. "Large-scale synthesis and functional elements for the antimicrobial activity of defensins." Biochemical Journal 347, no. 3 (April 25, 2000): 633–41. http://dx.doi.org/10.1042/bj3470633.
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