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Journal articles on the topic 'Thanatin'

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Author: Grafiati

Published: 9 March 2023

Last updated: 10 March 2023

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1

Ma, Bo, Chao Niu, Ying Zhou, Xiaoyan Xue, Jingru Meng, Xiaoxing Luo, and Zheng Hou. "The Disulfide Bond of the Peptide Thanatin Is Dispensible for Its Antimicrobial ActivityIn VivoandIn Vitro." Antimicrobial Agents and Chemotherapy 60, no. 7 (May 9, 2016): 4283–89. http://dx.doi.org/10.1128/aac.00041-16.

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ABSTRACTThanatin (THA) displays potent antibiotic activity, especially against extended-spectrum-β-lactamase (ESBL)-producingEscherichia colibothin vitroandin vivo, with minimal hemolytic toxicity and satisfactory stability in plasma. However, the high cost of thanatin significantly limits its development and clinical application. To reduce the cost of peptide synthesis, a formulation of cyclic thanatin (C-thanatin) called linear thanatin (L-thanatin) was synthesized and its activity was evaluatedin vivoandin vitro. Results showed that C-thanatin and L-thanatin MICs did not differ against eight Gram-negative and two Gram-positive bacterial strains. Furthermore, the survival rates of ESBL-producing-E. coli-infected mice were consistent after C-thanatin or L-thanatin treatment at 5 or 10 mg/kg of body weight. Neither C-thanatin nor L-thanatin showed toxicity for human red blood cells (hRBCs) and human umbilical vein endothelial cells (HUVECs) at a concentration as high as 256 μg/ml. Results of circular dichroism spectroscopy indicated that the secondary structure of L-thanatin is extremely similar to that of C-thanatin. Membrane permeabilization and depolarization assays showed that C-thanatin and L-thanatin have similar abilities to permeabilize the outer and inner membranes and to induce membrane depolarization in ESBL-producingE. coli. However, neither of them caused significant HUVEC membrane permeability. These findings indicate that the two peptides have similar effects on bacterial cell membranes and that the disulfide bond in thanatin is not essential for its antimicrobial activitiesin vivoandin vitro. L-thanatin is thus a promising low-cost peptide candidate for treating ESBL-producingE. coliinfections.

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2

Jackson, Karen E., and Tiffany Miller-White. "The intracellular target of the antimicrobial peptide thanatin." Journal of Immunology 200, no. 1_Supplement (May 1, 2018): 170.17. http://dx.doi.org/10.4049/jimmunol.200.supp.170.17.

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Abstract Thanatin is an inducible 21-residue antimicrobial peptide (AMP) derived from the insect Podisus maculiventris. Thanatin and its analogs have bactericidal activity against gram-positive and gram-negative bacteria, including antibiotic resistant strains. Due to the lack of hemolytic action, thanatin is a good candidate for therapeutic use, as evidenced by its ability to fight sepsis in mice. However, the mode of action of thanatin remains unexplored. Introduction of the respiratory poison carbonyl cyanide m-chlorophenyl hydrazone (CCCP) inhibits AMP induced death, suggesting that the bacterial respiratory pathway is targeted. In this study, biotinylated S-thanatin was used to determine a minimum inhibitory concentration (MIC) in Escherichia coli. Biotinylated S-thanatin showed comparable killing activity to the non-biotinylated peptide, 8μg/mL vs. 4μg/mL, respectively. Next, the killing activity of biotinylated S-thanatin was determined for cultures of E. coli grown under anaerobic, aerobic and respiratory dependent conditions. Anaerobic growth was shown to inhibit thanatin-induced microbial death, and respiratory dependent increased sensitivity. Currently, we are using biotinylated S-thanatin in an affinity purification assay to isolate the intracellular target to be analyzed using matrix assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectroscopy.

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3

Dash, Rachita, and Surajit Bhattacharjya. "Thanatin: An Emerging Host Defense Antimicrobial Peptide with Multiple Modes of Action." International Journal of Molecular Sciences 22, no. 4 (February 3, 2021): 1522. http://dx.doi.org/10.3390/ijms22041522.

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Antimicrobial peptides (AMPs) possess great potential for combating drug-resistant bacteria. Thanatin is a pathogen-inducible single-disulfide-bond-containing β-hairpin AMP which was first isolated from the insect Podisus maculiventris. The 21-residue-long thanatin displays broad-spectrum activity against both Gram-negative and Gram-positive bacteria as well as against various species of fungi. Remarkably, thanatin was found to be highly potent in inhibiting the growth of bacteria and fungi at considerably low concentrations. Although thanatin was isolated around 25 years ago, only recently has there been a pronounced interest in understanding its mode of action and activity against drug-resistant bacteria. In this review, multiple modes of action of thanatin in killing bacteria and in vivo activity, therapeutic potential are discussed. This promising AMP requires further research for the development of novel molecules for the treatment of infections caused by drug resistant pathogens.

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4

Zhang, Hongyan, Sha Liu, Xindan Li, Wenjun Wang, Lili Deng, and Kaifang Zeng. "Interaction of Antimicrobial Peptide Ponericin W1, Thanatin, and Mastatopara-S with Geotrichum citri-aurantii Genomic DNA." Foods 10, no. 8 (August 18, 2021): 1919. http://dx.doi.org/10.3390/foods10081919.

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Antimicrobial peptides of mastatopara-S (M-S), thanatin, and ponericin W1(P W1) were able to disrupt the membrane integrity and alter the morphology of the hyphae of Geotrichum citri-aurantii and then reduced the sour rot of citrus fruit. In order to understand the mechanisms of thanatin, P W1 and M-S other than membrane disruption, the interaction betwixt the peptides and G. citri-aurantii DNA were investigated in this research. The laser confocal microscopy found that P W1, thanatin, and M-S could penetrate the cell membrane. Gel retardation assay demonstrated that P W1, thanatin, and M-S could bind to the G. citri-aurantii genomic DNA in vitro. UV-visible spectra and fluorescence spectra analysis further confirmed that the peptides can bind to the DNA, and then insert into the base pairs in the DNA helix, followed by wrecking the double-helix structure. In addition, M-S, thanatin, and P W1 can suppress the synthesis of DNA and RNA of G. citri-aurantii.

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5

Tanhaeian, Abbas, Marjan Azghandi, Zahra Mousavi, and Ali Javadmanesh. "Expression of Thanatin in HEK293 Cells and Investigation of its Antibacterial Effects on Some Human Pathogens." Protein & Peptide Letters 27, no. 1 (December 10, 2019): 41–47. http://dx.doi.org/10.2174/0929866526666190822162140.

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Background: Thanatin is the smallest member of Beta-hairpin class of cationic peptide derived from insects with vast activities against various pathogens. Objective: n this study, the antimicrobial activity of this peptide against some species of human bacterial pathogens as well as its toxicity on NIH cells were evaluated. Method: Thanatin DNA sequence was cloned into pcDNA3.1+ vector and transformed into a DH5α bacterial strain. Then the recombinant plasmids were transfected into HEK-293 cells by calcium phosphate co-precipitation. After applying antibiotic treatment, the supernatant medium containing thanatin was collected. The peptide quantity was estimated by SDS-PAGE and GelQuant software. The antimicrobial activity of this peptide was performed with Minimum Inhibitory Concentration (MIC) method. In addition, its toxicity on NIH cells were evaluated by MTT assay. Results: The peptide quantity was estimated approximately 164.21 µmolL-1. The antibacterial activity of thanatin was estimated between 0.99 and 31.58 µmolL-1 using MIC method. The result of cytotoxicity test on NIH cell line showed that the peptide toxicity up to the concentration of 394.10 µmolL-1 and for 48 hours, was not statistically significant from negative control cells (P>0.05). The antimicrobial assay demonstrated that thanatin had an antibacterial effect on some tested microorganisms. The results obtained in this study also showed that thanatin had no toxicity on mammalian cell lines including HEK293 and NIH. Conclusion: Antimicrobial peptides such as thanatin are considered to be appropriate alternatives to conventional antibiotics in treating various human pathological diseases bacteria.

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6

Hou, Zheng, Fei Da, Baohui Liu, Xiaoyan Xue, Xiuli Xu, Ying Zhou, Mingkai Li, et al. "R-Thanatin Inhibits Growth and Biofilm Formation of Methicillin-Resistant Staphylococcus epidermidisIn VivoandIn Vitro." Antimicrobial Agents and Chemotherapy 57, no. 10 (August 5, 2013): 5045–52. http://dx.doi.org/10.1128/aac.00504-13.

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ABSTRACTStaphylococcus epidermidisis one of the most frequent causes of device-associated infections, because it is known to cause biofilms that grow on catheters or other surgical implants. The persistent increasing resistance ofS. epidermidisand other coagulase-negative staphylococci (CoNS) has driven the need for newer antibacterial agents with innovative therapeutic strategies. Thanatin is reported to display potent antibiotic activities, especially against extended-spectrum-beta-lactamase-producingEscherichia coli. The present study aimed to investigate whether a shorter derivative peptide (R-thanatin) could be used as a novel antibacterial agent. We found that R-thanatin was highly potentin vitroagainst coagulase-negative staphylococci, such asS. epidermidis,S. haemolyticus, andS. hominis, and inhibited biofilm formation at subinhibitory concentrations. Properties of little toxicity to human red blood cells (hRBCs) and human umbilical vein endothelial cells, a low incidence of resistance, and relatively high stability in plasma were confirmed. Excellentin vivoprotective effects were also observed using a methicillin-resistantS. epidermidis(MRSE)-induced urinary tract infection rat model. Electron microscopy and confocal laser-scanning microscopy analyses suggested that R-thanatin disturbed cell division of MRSE severely, which might be the reason for inhibition of MRSE growth. These findings indicate that R-thanatin is active against the growth and biofilm formation of MRSEin vitroandin vivo. R-thanatin might be considered as a specific drug candidate for treating CoNS infections.

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7

Wu, Guoqiu, Pengpeng Wu, Xiulei Xue, Xuejiao Yan, Siru Liu, Chen Zhang, Zilong Shen, and Tao Xi. "Application of S-thanatin, an antimicrobial peptide derived from thanatin, in mouse model of Klebsiella pneumoniae infection." Peptides 45 (July 2013): 73–77. http://dx.doi.org/10.1016/j.peptides.2013.04.012.

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8

Hongbiao, W., N. Baolong, H. Lihua, S. Weifeng, and M. Zhiqi. "Biological activities of cecropin B-thanatin hybrid peptides." Journal of Peptide Research 66, no. 6 (December 4, 2008): 382–86. http://dx.doi.org/10.1111/j.1399-3011.2005.00299.x.

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9

Koch, Aline, Walaa Khalifa, Gregor Langen, Andreas Vilcinskas, Karl-Heinz Kogel, and Jafargholi Imani. "The Antimicrobial Peptide Thanatin Reduces Fungal Infections in Arabidopsis." Journal of Phytopathology 160, no. 10 (July 12, 2012): 606–10. http://dx.doi.org/10.1111/j.1439-0434.2012.01946.x.

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10

Wu, Guoqiu, Hongbin Wu, Xiaobo Fan, Rui Zhao, Xiaofang Li, Shenglan Wang, Yihua Ma, Zilong Shen, and Tao Xi. "Selective toxicity of antimicrobial peptide S-thanatin on bacteria." Peptides 31, no. 9 (September 2010): 1669–73. http://dx.doi.org/10.1016/j.peptides.2010.06.009.

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11

Wu, Guoqiu, Jiaxuan Ding, Hui Li, Linxian Li, Rui Zhao, Zilong Shen, Xiaobo Fan, and Tao Xi. "Effects of Cations and PH on Antimicrobial Activity of Thanatin and s-Thanatin Against Escherichia coli ATCC25922 and B. subtilis ATCC 21332." Current Microbiology 57, no. 6 (September 23, 2008): 552–57. http://dx.doi.org/10.1007/s00284-008-9241-6.

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12

Wu, Guo-Qiu, Jia-Xuan Ding, Lin-Xian Li, Hai-liang Wang, Rui Zhao, and Zi-Long Shen. "Activity of the Antimicrobial Peptide and Thanatin Analog S-thanatin on Clinical Isolates of Klebsiella pneumoniae Resistant to Conventional Antibiotics with Different Structures." Current Microbiology 59, no. 2 (May 21, 2009): 147–53. http://dx.doi.org/10.1007/s00284-009-9410-2.

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13

Wu, Guoqiu, Xuepeng Deng, Pengpeng Wu, Zilong Shen, and Hanmei Xu. "Subacute toxicity of antimicrobial peptide S-thanatin in ICR mice." Peptides 36, no. 1 (July 2012): 109–13. http://dx.doi.org/10.1016/j.peptides.2012.04.005.

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14

Schubert, Max, Marcel Houdelet, Karl-Heinz Kogel, Rainer Fischer, Stefan Schillberg, and Greta Nölke. "Thanatin confers partial resistance against aflatoxigenic fungi in maize (Zea mays)." Transgenic Research 24, no. 5 (June 13, 2015): 885–95. http://dx.doi.org/10.1007/s11248-015-9888-2.

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15

Miao, Xiang-Yang, and Xin Zhang. "Production of transgenic mice carrying the Thanatin gene by intratesticular injection." Biochemical and Biophysical Research Communications 415, no. 3 (November 2011): 429–33. http://dx.doi.org/10.1016/j.bbrc.2011.10.044.

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16

Wu, Guoqiu, Hongbin Wu, Linxian Li, Xiaobo Fan, Jiaxuan Ding, Xiaofang Li, Tao Xi, and Zilong Shen. "Membrane aggregation and perturbation induced by antimicrobial peptide of S-thanatin." Biochemical and Biophysical Research Communications 395, no. 1 (April 2010): 31–35. http://dx.doi.org/10.1016/j.bbrc.2010.03.107.

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17

Vetterli, Stefan U., Katja Zerbe, Maik Müller, Matthias Urfer, Milon Mondal, Shuang-Yan Wang, Kerstin Moehle, et al. "Thanatin targets the intermembrane protein complex required for lipopolysaccharide transport inEscherichia coli." Science Advances 4, no. 11 (November 2018): eaau2634. http://dx.doi.org/10.1126/sciadv.aau2634.

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With the increasing resistance of many Gram-negative bacteria to existing classes of antibiotics, identifying new paradigms in antimicrobial discovery is an important research priority. Of special interest are the proteins required for the biogenesis of the asymmetric Gram-negative bacterial outer membrane (OM). Seven Lpt proteins (LptA to LptG) associate in most Gram-negative bacteria to form a macromolecular complex spanning the entire envelope, which transports lipopolysaccharide (LPS) molecules from their site of assembly at the inner membrane to the cell surface, powered by adenosine 5′-triphosphate hydrolysis in the cytoplasm. The periplasmic protein LptA comprises the protein bridge across the periplasm, which connects LptB2FGC at the inner membrane to LptD/E anchored in the OM. We show here that the naturally occurring, insect-derived antimicrobial peptide thanatin targets LptA and LptD in the network of periplasmic protein-protein interactions required to assemble the Lpt complex, leading to the inhibition of LPS transport and OM biogenesis inEscherichia coli.

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18

Akhlaghi, Mahdi, Saeed Tarighi, and Parissa Taheri. "Effect of antimicrobial peptides and monoterpenes on control of fire blight." Spanish Journal of Agricultural Research 18, no. 2 (April 8, 2020): e1002. http://dx.doi.org/10.5424/sjar/2020182-15629.

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Aim of study: Antimicrobial peptides and monoterpenes are safe compounds that have been used for control of many plant diseases. Herein, the effects of two recombinant antibacterial peptides (AMPs) were compared with two monoterpenes for control of Erwinia amylovora directly or via induction of plant defense enzyme guaiacol peroxidase (GPOD).Area of study: The experiments were performed at the Ferdowsi University of Mashhad (Iran).Material and methods: The central composite design (CCD) method was used to study the effect of mixing the compounds and copper compound (Nordox) in controlling the pathogen. The resistance level was studied on shoots of tolerant (‘Dargazi’) and semi-susceptible (‘Spadona’) pear cultivars treated with the antibacterial compounds.Main results: Thanatin and 1,8-cineole showed the highest and lowest antibacterial effects. All treatments reduced E. amylovora pathogenicity on blossom. The CCD analysis revealed that the best reduction in colony number obtained by mixing Lfc, thanatin, thymol, 1,8-cineole and Nordox at concentrations of 32, 16, 24, 250 and 250 μg/mL. Thymol and 1,8-cineole at 500 μg/mL decreased disease severity significantly compared to that of AMPs. The level of GPOD enzyme in ‘Dargazi’ was higher than in ‘Spadona’. All treatments increased the GPOD levels in both cultivars. Furthermore, resistance level and GPOD ratio were negatively correlated.Research highlights: Antimicrobial peptides showed better effect on growth inhibition of E. amylovora than monoterpenes. Mixing of these peptides and monoterpens at special dosage enhanced their antimicrobial efficacy against E. amylovora; that could represent a new method in control of fire blight disease.

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19

Schwinges, Patrick, Shyam Pariyar, Felix Jakob, Mehran Rahimi, Lina Apitius, Mauricio Hunsche, Lutz Schmitt, et al. "A bifunctional dermaseptin–thanatin dipeptide functionalizes the crop surface for sustainable pest management." Green Chemistry 21, no. 9 (2019): 2316–25. http://dx.doi.org/10.1039/c9gc00457b.

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20

Pagès, J. "Thanatin activity on multidrug resistant clinical isolates of Enterobacter aerogenes and Klebsiella pneumoniae." International Journal of Antimicrobial Agents 22, no. 3 (September 2003): 265–69. http://dx.doi.org/10.1016/s0924-8579(03)00201-2.

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21

Rothan, Hussin A., Hirbod Bahrani, Esaki M. Shankar, Noorsaadah Abd Rahman, and Rohana Yusof. "Inhibitory effects of a peptide-fusion protein (Latarcin–PAP1–Thanatin) against chikungunya virus." Antiviral Research 108 (August 2014): 173–80. http://dx.doi.org/10.1016/j.antiviral.2014.05.019.

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22

Andrès, E. "Cationic antimicrobial peptides in clinical development, with special focus on thanatin and heliomicin." European Journal of Clinical Microbiology & Infectious Diseases 31, no. 6 (October 1, 2011): 881–88. http://dx.doi.org/10.1007/s10096-011-1430-8.

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23

Miao, Xiangyang, Xin Zhang, and Ruijie Zhang. "Production of Transgenic Sheep Carrying Thanatin Gene by Transfection of Spermatogonial Stem Cells." Biology of Reproduction 85, Suppl_1 (July 1, 2011): 178. http://dx.doi.org/10.1093/biolreprod/85.s1.178.

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24

Park, Kyoung-Eun, Seong Han Jang, Junbeom Lee, Seung Ah Lee, Yoshitomo Kikuchi, Young-su Seo, and Bok Luel Lee. "The roles of antimicrobial peptide, rip-thanatin, in the midgut of Riptortus pedestris." Developmental & Comparative Immunology 78 (January 2018): 83–90. http://dx.doi.org/10.1016/j.dci.2017.09.009.

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25

Wu, Guoqiu, Xuepeng Deng, Xiaofang Li, Xiyong Wang, Shenglan Wang, and Hanmei Xu. "Application of immobilized thrombin for production of S-thanatin expressed in Escherichia coli." Applied Microbiology and Biotechnology 92, no. 1 (June 8, 2011): 85–93. http://dx.doi.org/10.1007/s00253-011-3379-z.

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26

Wang, Li Na, Bing Yu, Guo Quan Han, Jun He, and Dai Wen Chen. "Design, expression and characterization of recombinant hybrid peptide Attacin-Thanatin in Escherichia coli." Molecular Biology Reports 37, no. 7 (December 5, 2009): 3495–501. http://dx.doi.org/10.1007/s11033-009-9942-3.

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27

Liu, Zeqiang, Mingxing Zhu, Xiangjun Chen, Guimao Yang, Tiantian Yang, Longmei Yu, Liyuan Hui, and Xiuqing Wang. "Expression and antibacterial activity of hybrid antimicrobial peptide cecropinA-thanatin in Pichia pastoris." Frontiers in Laboratory Medicine 2, no. 1 (March 2018): 23–29. http://dx.doi.org/10.1016/j.flm.2018.04.001.

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28

Tian, Lu, Di Zhang, Peng Su, Yuan Wei, Zhongzhong Wang, Pan Xue Wang, Chun Ji Dai, and Guo Li Gong. "Design, recombinant expression, and antibacterial activity of a novel hybrid magainin–thanatin antimicrobial peptide." Preparative Biochemistry & Biotechnology 49, no. 5 (March 12, 2019): 427–34. http://dx.doi.org/10.1080/10826068.2018.1476875.

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29

Imamura, Tomohiro, Michiko Yasuda, Hiroaki Kusano, Hideo Nakashita, Yuko Ohno, Takashi Kamakura, Seiichi Taguchi, and Hiroaki Shimada. "Acquired resistance to the rice blast in transgenic rice accumulating the antimicrobial peptide thanatin." Transgenic Research 19, no. 3 (September 27, 2009): 415–24. http://dx.doi.org/10.1007/s11248-009-9320-x.

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30

WANG, Xiao-Fu. "Construction of vectors for expression of cleavable tandem repeat Thanatin fusion protein in plants." HEREDITAS 29, no. 06 (2007): 758. http://dx.doi.org/10.1360/yc-007-0758.

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31

Wu, G. Q., L. X. Li, J. X. Ding, L. Z. Wen, and Z. L. Shen. "High-Level Expression and Novel Purification Strategy of Recombinant Thanatin Analog in Escherichia coli." Current Microbiology 57, no. 2 (June 6, 2008): 95–101. http://dx.doi.org/10.1007/s00284-008-9106-z.

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32

Lee, Myung-Kyu, Li-Na Cha, Si-Hyung Lee, and Kyung-Soo Hahm. "Role of Amino Acid Residues within the Disulfide Loop of Thanatin, a Potent Antibiotic Peptide." BMB Reports 35, no. 3 (May 31, 2002): 291–96. http://dx.doi.org/10.5483/bmbrep.2002.35.3.291.

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33

Cirioni, Oscar, Guoqiu Wu, Linxian Li, Fiorenza Orlando, Carmela Silvestri, Roberto Ghiselli, Zilong Shen, et al. "S-thanatin enhances the efficacy of tigecycline in an experimental rat model of polymicrobial peritonitis." Peptides 31, no. 7 (July 2010): 1231–36. http://dx.doi.org/10.1016/j.peptides.2010.03.034.

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34

Wu, Guoqiu, Xiaofang Li, Xuepeng Deng, Xiaobo Fan, Shenglan Wang, Zilong Shen, and Tao Xi. "Protective effects of antimicrobial peptide S-thanatin against endotoxic shock in mice introduced by LPS." Peptides 32, no. 2 (February 2011): 353–57. http://dx.doi.org/10.1016/j.peptides.2010.10.029.

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35

Wu, Guoqiu, Xiaofang Li, Xiaobo Fan, Hongbin Wu, Shenglan Wang, Zilong Shen, and Tao Xi. "The activity of antimicrobial peptide S-thanatin is independent on multidrug-resistant spectrum of bacteria." Peptides 32, no. 6 (June 2011): 1139–45. http://dx.doi.org/10.1016/j.peptides.2011.03.019.

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36

Wu, Guoqiu, Shenglan Wang, Xiyong Wang, Xiaofang Li, Xuepeng Deng, Zilong Shen, and Tao Xi. "Determination of a new antibacterial peptide S-thanatin in rat plasma by an indirected-ELISA." Peptides 32, no. 7 (July 2011): 1484–87. http://dx.doi.org/10.1016/j.peptides.2011.05.009.

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37

Robert, Émile, Thierry Lefèvre, Matthieu Fillion, Benjamin Martial, Justine Dionne, and Michèle Auger. "Mimicking and Understanding the Agglutination Effect of the Antimicrobial Peptide Thanatin Using Model Phospholipid Vesicles." Biochemistry 54, no. 25 (June 19, 2015): 3932–41. http://dx.doi.org/10.1021/acs.biochem.5b00442.

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38

Robert, Émile, Thierry Lefèvre, Matthieu Fillion, Benjamin Martial, Justine Dionne, and Michèle Auger. "Mimicking and Understanding the Agglutination Effect of the Antimicrobial Peptide Thanatin using Model Phospholipid Vesicles." Biophysical Journal 110, no. 3 (February 2016): 416a. http://dx.doi.org/10.1016/j.bpj.2015.11.2251.

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39

Wu, Tingquan, Dingzhong Tang, Weida Chen, Hexun Huang, Rui Wang, and Yongfang Chen. "Expression of antimicrobial peptides thanatin(S) in transgenic Arabidopsis enhanced resistance to phytopathogenic fungi and bacteria." Gene 527, no. 1 (September 2013): 235–42. http://dx.doi.org/10.1016/j.gene.2013.06.037.

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40

Bhattacharjya, Surajit, Sk Abdul Mohid, and Anirban Bhunia. "Atomic-Resolution Structures and Mode of Action of Clinically Relevant Antimicrobial Peptides." International Journal of Molecular Sciences 23, no. 9 (April 20, 2022): 4558. http://dx.doi.org/10.3390/ijms23094558.

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Global rise of infections and deaths caused by drug-resistant bacterial pathogens are among the unmet medical needs. In an age of drying pipeline of novel antibiotics to treat bacterial infections, antimicrobial peptides (AMPs) are proven to be valid therapeutics modalities. Direct in vivo applications of many AMPs could be challenging; however, works are demonstrating encouraging results for some of them. In this review article, we discussed 3-D structures of potent AMPs e.g., polymyxin, thanatin, MSI, protegrin, OMPTA in complex with bacterial targets and their mode of actions. Studies on human peptide LL37 and de novo-designed peptides are also discussed. We have focused on AMPs which are effective against drug-resistant Gram-negative bacteria. Since treatment options for the infections caused by super bugs of Gram-negative bacteria are now extremely limited. We also summarize some of the pertinent challenges in the field of clinical trials of AMPs.

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41

Robert, Émile, Matthieu Fillion, François Otis, Normand Voyer, and Michèle Auger. "Understanding How the Antimicrobial Peptide Thanatin Interacts with the Lipid Bilayer of Cell Walls Using Model Membranes." Biophysical Journal 106, no. 2 (January 2014): 85a. http://dx.doi.org/10.1016/j.bpj.2013.11.546.

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42

Imamura, Tomohiro, Ken-Taro Sekine, Tetsuro Yamashita, Hiroaki Kusano, and Hiroaki Shimada. "Production of recombinant thanatin in watery rice seeds that lack an accumulation of storage starch and proteins." Journal of Biotechnology 219 (February 2016): 28–33. http://dx.doi.org/10.1016/j.jbiotec.2015.12.006.

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43

Sinha, Sheetal, Vidhya Bharathi Dhanabal, Paola Sperandeo, Alessandra Polissi, and Surajit Bhattacharjya. "Linking dual mode of action of host defense antimicrobial peptide thanatin: Structures, lipopolysaccharide and LptAm binding of designed analogs." Biochimica et Biophysica Acta (BBA) - Biomembranes 1864, no. 3 (March 2022): 183839. http://dx.doi.org/10.1016/j.bbamem.2021.183839.

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44

Cirioni, Oscar, Guoqiu Wu, Linxian Li, Fiorenza Orlando, Carmela Silvestri, Roberto Ghiselli, Zilong Shen, et al. "S-thanatin in vitro prevents colistin resistance and improves its efficacy in an animal model of Pseudomonas aeruginosa sepsis." Peptides 32, no. 4 (April 2011): 697–701. http://dx.doi.org/10.1016/j.peptides.2011.01.016.

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45

Sinha, Sheetal, Wun Jern Ng, and Surajit Bhattacharjya. "NMR structure and localization of the host defense antimicrobial peptide thanatin in zwitterionic dodecylphosphocholine micelle: Implications in antimicrobial activity." Biochimica et Biophysica Acta (BBA) - Biomembranes 1862, no. 11 (November 2020): 183432. http://dx.doi.org/10.1016/j.bbamem.2020.183432.

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Taguchi, S., K. Kuwasako, A. Suenaga, M. Okada, and H. Momose. "Functional Mapping against Escherichia coli for the Broad-Spectrum Antimicrobial Peptide, Thanatin, Based on an In Vivo Monitoring Assay System." Journal of Biochemistry 128, no. 5 (November 1, 2000): 745–54. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a022811.

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ORIKASA, Yoshitake, Kenta ICHINOHE, Junki SAITO, Shigeki HASHIMOTO, Ken’ichiro MATSUMOTO, Toshihiko OOI, and Seiichi TAGUCHI. "The Hydrophobicity in a Chemically Modified Side-Chain of Cysteine Residues of Thanatin Is Related to Antimicrobial Activity againstMicrococcus luteus." Bioscience, Biotechnology, and Biochemistry 73, no. 7 (July 23, 2009): 1683–84. http://dx.doi.org/10.1271/bbb.90183.

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Zhou, Quan, Huimin Fan, Peifeng Lu, Yuyan Zhou, Wei Li, and Jianhua Liu. "Linear Thanatin Is an Effective Antimicrobial Peptide against Colistin-Resistant <i>Escherichia coli in Vitro</i>." Advances in Microbiology 08, no. 07 (2018): 589–99. http://dx.doi.org/10.4236/aim.2018.87039.

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Mandard, Nicolas, Patrick Sodano, Henri Labbe, Jean-Marc Bonmatin, Philippe Bulet, Charles Hetru, Marius Ptak, and Francoise Vovelle. "Solution structure of thanatin, a potent bactericidal and fungicidal insect peptide, determined from proton two-dimensional nuclear magnetic resonance data." European Journal of Biochemistry 256, no. 2 (September 1998): 404–10. http://dx.doi.org/10.1046/j.1432-1327.1998.2560404.x.

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Fehlbaum, P., P. Bulet, S. Chernysh, J. P. Briand, J. P. Roussel, L. Letellier, C. Hetru, and J. A. Hoffmann. "Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides." Proceedings of the National Academy of Sciences 93, no. 3 (February 6, 1996): 1221–25. http://dx.doi.org/10.1073/pnas.93.3.1221.

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