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Letters in Organic Chemistry

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ISSN (Print): 1570-1786
ISSN (Online): 1875-6255

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Research Article

In-silico Approach for Evaluation of Antimalarial Potential of Costunolide Synthase Enzyme and Sesquiterpene Lactones from Cichorium intybus

Author(s): Abhishek Pathak, Sunita Arora, Apoorv Tiwari, Kurma Dev Krishna, S.P. Singh and Gohar Taj*

Volume 20, Issue 1, 2023

Published on: 19 August, 2022

Page: [61 - 71] Pages: 11

DOI: 10.2174/1570178619666220608113803

Price: $65

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Abstract

Background: Cichorium intybus is a perennial herb in the Asteraceae family that has significant ethano-medical properties and is utilized in Ayurveda and Unani therapy. The enzyme costunolide synthase contributes to the biosynthesis pathway of sesquiterpene lactones, which is thought to provide the plant with antimalarial action.

Methods: This work uses several in-silico techniques along with docking experiments to show the structural and physiochemical characteristics of the enzyme costunolide synthase. Costunolide synthase protein interacts with lactucin and lactucopicrin with lower energy interactions of -4.99 kcal/mol for total 3 hydrogen bonds and -6.55 kcal/mol for total 2 hydrogen bonds, respectively. One domain named CYP 450 has been found, which catalyzes a variety of oxidative reactions of a large number of structurally different compounds that are both endogenous and exogenous from all major domains of life. The mitochondrial cellular localization of protein was revealed with a maximum score of 1.833.

Results: The phylogenetic study revealed that the enzyme costunolide synthase from Cichorium intybus has a greater resemblance to Cichorium endivia and Lactuca sativa of costunolide synthase. Molecular docking findings of sesquiterpene lactones (lactucin and lactucopicrin) with Plasmepsin II protein of P. falciparum parasites after clinical trials with sesquiterpene lactones may give more evidence and explanation for the active involvement of lactucin and lactucopicrin as an antimalarial compound.

Conclusion: This research will be used in future wet-lab studies to figure out how the costunolide synthase enzyme regulates sesquiterpene lactones and to investigate additional regulatory enzyme involved in the synthesis of sesquiterpene lactones.

Keywords: Sesquiterpene lactones, lactucin, lactucopicrin, antimalarial agent, molecular docking, plasmepsin II.

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[1]
Das, S.; Vasudeva, N.; Sharma, S. Drug Devepl. Ther., 2016, 7, 1-12.
[http://dx.doi.org/10.4103/2394-6555.180157]
[2]
Street, A.R.; Sidana, J.; Prinslo, G. Evid. Based Complement. Alternat. Med., 2013, 10, 1155.
[3]
Thorat, B.S.; Raut, S.M. J. Medic. Plants Stud., 2018, 6, 49-52.
[4]
Bais, P.H.; Ravishankar, G.A. J. Sci. Food Agric., 2001, 81, 467-484.
[http://dx.doi.org/10.1002/jsfa.817]
[5]
Maurice, D.P.; Nico, V.S.; Noten, V. Breeding and cultivar identification of Cichorium intybus L. var. Foliosum hegi. Eucarpia Leafy Vegetables. Centre for Genetic Resources; CGN: The Netherlands, 2003, pp. 83-90.
[6]
Zaman, R.A. Res. J. Pharm., 2013, 23, 555-576.
[7]
Ying, G.W.; Gui, L.J. J. Anim. Plant Sci., 2012, 13, 1736-1746.
[8]
Peters, A.M.; Van, A.A. J. Am. Soc. Hortic. Sci., 1998, 123, 326-329.
[http://dx.doi.org/10.21273/JASHS.123.2.326]
[9]
Testone, G.; Mele, G.; Di Giacomo, E.; Gonnella, M.; Renna, M.; Tenore, G.C.; Nicolodi, C.; Frugis, G.; Iannelli, M.A.; Arnesi, G.; Schiappa, A.; Giannino, D. Front. Plant Sci., 2017, 8, 478.
[http://dx.doi.org/10.3389/fpls.2017.00478] [PMID: 28396680]
[10]
Bischof, A.T.; Kelley, J.C.; Karchesy, Y. J. Inter. Ethnopharm., 2005, 95, 455-457.
[http://dx.doi.org/10.1016/j.jep.2004.06.031]
[11]
Channotiya, J.; Tiwari, A.; Taj, G.; Verma, A.K.; Dubey, A. Netw. Model. Anal. Health Inform. Bioinform., 2021, 10, 24.
[http://dx.doi.org/10.1007/s13721-021-00288-5]
[12]
Bharel, S.; Gulati, A.; Abdin, M.Z.; Srivastava, P.S.; Jain, S.K. Fitoterapia, 2012, 67, 387-399.
[13]
Banerjee, R.; Liu, J.; Beatty, W.; Pelosof, L.; Klemba, M.; Goldberg, D.E. Proc. Natl. Acad. Sci. USA, 2002, 99(2), 990-995.
[http://dx.doi.org/10.1073/pnas.022630099] [PMID: 11782538]
[14]
Cheuka, P.M.; Dziwornu, G.; Okombo, J.; Chibale, K. J. Med. Chem., 2020, 63(9), 4445-4467.
[http://dx.doi.org/10.1021/acs.jmedchem.9b01622] [PMID: 31913032]
[15]
Cruz, L.R.; Spangenberg, T.; Lacerda, M.V.G.; Wells, T.N.C.; Malar, J. 2013, 12, 168.
[http://dx.doi.org/10.1186/1475-2875-12-168] [PMID: 23706107]
[16]
Amoa Onguéné, P.; Ntie-Kang, F.; Lifongo, L.L.; Ndom, J.C.; Sippl, W.; Mbaze, L.M. Malar. J., 2013, 12, 449.
[http://dx.doi.org/10.1186/1475-2875-12-449] [PMID: 24330395]
[17]
Wells, T.N.C.; Malar, J. 2011, 10(Suppl. 1), S3.
[http://dx.doi.org/10.1186/1475-2875-10-S1-S3] [PMID: 21411014]
[18]
Guruprasad, K.; Reddy, B.V.; Pandit, M.W. Protein Eng., 1990, 4(2), 155-161.
[http://dx.doi.org/10.1093/protein/4.2.155] [PMID: 2075190]
[19]
Chang, K.Y.; Yang, J.R. PLoS One, 2013, 8(8), e70166.
[http://dx.doi.org/10.1371/journal.pone.0070166] [PMID: 23940542]
[20]
Dayton, W.R. Reciprocal Meat Confer. Proc., 1983, 36, 98-102.
[21]
Taylor, W.R.; White, N.J. Drug Saf., 2004, 27(1), 25-61.
[http://dx.doi.org/10.2165/00002018-200427010-00003] [PMID: 14720085]
[22]
Leonardi, E.; Gilvary, G.; White, N.J.; Nosten, F. Trans. R. Soc. Trop. Med. Hyg., 2001, 95(2), 182-183.
[http://dx.doi.org/10.1016/S0035-9203(01)90157-9] [PMID: 11355556]
[23]
Kumar, S.; Stecher, G.; Li, M.; Knyaz, C.; Tamura, K. Mol. Biol. Evol., 2018, 35(6), 1547-1549.
[http://dx.doi.org/10.1093/molbev/msy096] [PMID: 29722887]
[24]
(a) Yu, C.S.; Lin, C.J.; Hwang, J.K. Protein Sci., 2004, 13(5), 1402-1406.
[http://dx.doi.org/10.1110/ps.03479604] [PMID: 15096640];
(b) Yu, C.S.; Chen, Y.C.; Lu, C.H.; Hwang, J.K. Proteins, 2006, 64(3), 643-651.
[http://dx.doi.org/10.1002/prot.21018] [PMID: 16752418]
[25]
Dundas, J.; Ouyang, Z.; Tseng, J.; Binkowski, A.; Turpaz, Y.; Liang, J. Nucleic Acids Res., 2006, 34(Web Server issue), W116-8.
[http://dx.doi.org/10.1093/nar/gkl282] [PMID: 16844972]
[26]
Letunic, I.; Bork, P. Nucleic Acids Res., 2018, 46(D1), D493-D496.
[http://dx.doi.org/10.1093/nar/gkx922] [PMID: 29040681]
[27]
Marchler-Bauer, A.; Bo, Y.; Han, L.; He, J.; Lanczycki, C.J.; Lu, S.; Chitsaz, F.; Derbyshire, M.K.; Geer, R.C.; Gonzales, N.R.; Gwadz, M.; Hurwitz, D.I.; Lu, F.; Marchler, G.H.; Song, J.S.; Thanki, N.; Wang, Z.; Yamashita, R.A.; Zhang, D.; Zheng, C.; Geer, L.Y.; Bryant, S.H. Nucleic Acids Res., 2017, 45(D1), D200-D203.
[http://dx.doi.org/10.1093/nar/gkw1129] [PMID: 27899674]
[28]
Tiwari, A.; Avashthi, H.; Jha, R.; Srivastava, A.; Garg, V.K.; Ramteke, P.w.; Kumar, A. Bioinfor, 2016, 12, 3.
[http://dx.doi.org/10.6026/97320630012156]
[29]
Wang, S.; Li, W.; Liu, S.; Xu, J. Nucleic Acids Res., 2016, 44(W1), W430-5.
[http://dx.doi.org/10.1093/nar/gkw306] [PMID: 27112573]
[30]
Selvam, K.; Senbagam, D.; Selvankumar, T. J. Mol. Struct., 2017, 1150, 61-67.
[http://dx.doi.org/10.1016/j.molstruc.2017.08.067]
[31]
Ramachandran, G.N.; Ramakrishnan, C.; Sasisekharan, V. J. Mol. Biol., 1963, 7, 95-99.
[http://dx.doi.org/10.1016/S0022-2836(63)80023-6] [PMID: 13990617]
[32]
Castrignanò, T.; De Meo, P.D.; Cozzetto, D.; Talamo, I.G.; Tramontano, A. Nucleic Acids Res., 2006, 34, D306-D309.
[http://dx.doi.org/10.1093/nar/gkj105] [PMID: 16381873]
[33]
Szklarczyk, D.; Franceschini, A.; Wyder, S.; Forslund, K.; Heller, D.; Huerta-Cepas, J.; Simonovic, M.; Roth, A.; Santos, A.; Tsafou, K.P.; Kuhn, M.; Bork, P.; Jensen, L.J.; von Mering, C. Nucleic Acids Res., 2015, 43, D447-D452.
[http://dx.doi.org/10.1093/nar/gku1003] [PMID: 25352553]
[34]
Naik, P.A.; Zu, J. J. Bioinform. Comput. Biol., 2020, 18(2), 2050013.
[http://dx.doi.org/10.1142/S0219720020500134] [PMID: 32372713]

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