Соединения палладия - ингибиторы ферментов (обзор литературы)
DOI:
https://doi.org/10.7242/2658-705X/2021.4.1Ключевые слова:
абиогенез, генетический код, протобиомономеры, свойства аминокислот и нуклеотидных основанийАннотация
В настоящем обзоре собраны литературные данные 1969-2021 гг., направленные на изучение координационного окружения палладия в транс-координированных, бидентатных N, S, фосфиновых и иминофенольных комплексных соединениях металла, а также селективного воздействия палладия при ингибировании ферментативной активности и возможного проявления его токсичности. Показано, что соединения палладия ингибируют ферменты, участвующие в патогенезе ряда заболеваний, таких как болезнь Альцгеймера, Паркинсона, атеросклероз и сахарный диабет второго типа. Соединения палладия могут применяться в таргетной терапии рака не только по механизму воздействия на молекулу ДНК, но и в качестве ингибиторов опухолевых ферментов. Также известно, что соединения палладия могут использоваться в качестве ингибиторов ферментов вирусов ВИЧ-1, SARS-CoV-2, возбудителя сонной болезни, гнилостных бактерий и других микроорганизмов. В то же время некоторые комплексы палладия являются потенциальными токсинами и аллергенами из-за ингибирования ферментов, необходимых для нормального метаболизма. В данном обзоре обращено особое внимание на работы ученых Пермского федерального исследовательского центра УрО РАН, посвященные ингибированию моноаминоксидаз, участвующих в развитии болезни Паркинсона. Нами отмечено, что поиск новых комплексов палладия является перспективным направлением для биомедицины.
Библиографические ссылки
- Rosenberg B., VanCamp L., Trosko J.E., Mansour V.H. Platinum Compounds: a New Class of Potent Antitumour Agents // Nature. – 1969. – Vol. 222. – № 5191. – P. 385–386.
- Kilpin K.J., Dyson P.J. Enzyme inhibition by metal complexes: concepts, strategies and applications // Chemical Science. – 2013. – Vol. 4. – P. 1410–1419.
- Энциклопедия лекарственных препаратов РЛС [Электронный ресурс] – URL: https://www.rlsnet.ru/ (дата обращения: 26.05.2021).
- Shu X., Xiong X., Song J, He Ch., Yi Ch. Base Resolution Analysis of Cisplatin–DNA Adducts at the Genome Scale // Angewandte Chemie International Edition. – 2016. – Vol. 55. – № 46. – P. 14246–14249.
- Egorova K.S., Galushko A.S., Ananikov V.P. Introducing tox Profiles of Chemical Reactions // Angewandte Chemie International Edition. – 2020. – Vol. 59. – № 50. – P. 22296–22305.
- Dyson P.J., Sava G. Metal based antitumour drugs in the post genomic era // Dalton Transactions. – 2006. – Vol. 50. – № 16. – P. 1929–1933.
- Sava G., Bergamo A., Dyson P.J. Metal based antitumour drugs in the post genomic era: what comes
next? // Dalton Transactions. – 2011. – Vol. 40. – № 36. – P. 9069–9075.Ang W.H., Dyson P.J. Classical and Non Classical Ruthenium Based Anticancer Drugs: Towards Targeted Chemotherapy // European Journal of Inorganic Chemistry. – 2006. – Vol. 2006. – № 20. – P. 3993.Timerbaev A.R., Hartinger C.G., Aleksenko S.S., Keppler B.K. Interactions of Antitumor Metallodrugs with Serum Proteins: Advances in Characterization Using Modern Analytical Methodology // Chemical Reviews. – 2006. – Vol. 106. – № 6. – P. 2224–2248.Mulcahy S.P., Li S., Korn R., Xie X., Meggers E. Solid Phase Synthesis of Tris heteroleptic Ruthenium(II) Complexes and Application to Acetylcholinesterase Inhibition // Inorganic Chemistry. – 2008. – Vol. 47. – № 12. – P. 5030–5032.Ong J.X., Yap C.W., Ang W.H. Rational Design of Selective Organoruthenium Inhibitors of Protein Tyrosine Phosphatase 1B // Inorganic Chemistry. – 2012. – Vol. 51. – № 22. – P. 12483–12492.Liu W., Gust R. Update on metal N heterocyclic carbene complexes as potential anti-tumor metallodrugs // Coordinational Chemistry Reviews. – 2016. – Vol. 329. – № 15. – P. 191–213.Soman S., Keatinge M., Moein M., Costa M.C., Mortiboys H., Skupin A., Sugunan S., Bazala M., Kuznicki J., Bandmann O. Inhibition of the mitochondrial calcium uniporter rescues dopaminergic neurons in pink1−/− zebrafish // European Journal of Neuro science. – 2017. – Vol. 45. – № 4 – P. 528–535.Meggers E. From Conventional to Unusual Enzyme Inhibitor Scaffolds: The Quest for Target Specificity // Angewandte Chemie International Edition. – 2011. – Vol. 50. – № 11. – P. 2442–2448.Che C.-M., Siu F.-M. Metal complexes in medicine with a focus on enzyme inhibition // Current
Opinion in Chemical Biology. – 2010. – Vol. 14. – № 2 – P. 255–261.Bruijnincx P.C.A., Sadler P.J. New trends for metal complexes with anticancer activity // Current Opinion in Chemical Biology. – 2008. – Vol. 12. – № 2 – P. 197–206.Louie A.Y., Meade T.J. Metal Complexes as Enzyme Inhibitors // Chemistry Reviews. – 1999. – Vol. 99. – № 9 – P. 2711–2734.Meggers E. Targeting proteins with metal complexes // Chemical Communications. – 2009. – Vol. 45. – № 9 – P. 1001–1010. Abu Surrah A.S., Al Sa’doni H.H., Abdalla M.Y. Palladium based chemotherapeutic agents: Routes toward complexes with good antitumor activity // Cancer Therapy. – 2008. – Vol. 6. – P. 1–10.Marques M.P.M. Platinum and Palladium Polyamine Complexes as Anticancer Agents: The Structural Factor // International Scholarly Research Notices Spectroscopy. – 2013. – Vol. 2013. – P. 1–29.Jahromi E.Z., Divsalar A., Saboury A.A., Khaleghizadeh S., Mansouri Torshizi H., Kostova I. Palladium complexes: new candidates for anticancer drugs // Journal of the Iranian Chemical Society. – 2016. – Vol. 13. – P. 967–989.Carneiro T.J., Martins A.S., Marques M.P.M., Gil A.M. Metabolic Aspects of Palladium(II) Potential Anti-Cancer Drugs // Frontiers in Oncology. – 2020. – Vol. 10. – №. 590970 DOI: 10.3389/fonc.2020.590970. Залевская О.А., Гурьева Я.А., Кучин А.В. Терпеновые лиганды в координационной химии: синтез металлокомплексных соединений, стереохимия, каталитические свойства, биологическая активность // Успехи химии. – 2019. – Т. 88. – № 10 – С. 979–1012.Денисов М.С., Глушков В.А. Биологически активные комплексы палладия(II) и N гетероциклических ароматических лигандов (обзор литературы) // Вестник Пермского университета. Серия «Химия». – 2018. – Т. 8. – № 4. – P. 388–411.Serratrice M., Maiore L., Zucca A., Stoccoro S., Landini I., Mini E., Massai L., Ferraro G., Merlino A., Messori L., Cinellu M.A. Cytotoxic properties of a new organometallic platinum(II) complex and its gold(I) heterobimetallic derivatives // Dalton Transactions. – 2016. – Vol. 45. – № 2. – P. 579–590.Mitr I., Mukherjee S., Reddy B. V.P., Misini B., Das P., Dasgupta S., Linert W., Moi S.Ch. Synthesis, biological evaluation, substitution behaviour and DFT study of Pd(II) complexes incorporating benzimidazole derivative // New Journal of Chemistry. – 2018. – Vol. 42. – № 2. – P. 2574–2589. Aghatabay N.M., Somer M., Senel M., Dulger B., Gucin. F. Raman, FT IR, NMR spectroscopic data and antimicrobial activity of bis[μ2 (benzimidazol 2 yl) 2 ethanethiolato N,S,S chloro-palladium(II)] dimer, [(μ2 CH2CH2NHNCC6H4)PdCl]2•C2H5OH complex // European Journal of Medicinal Chemistry. – 2007. – Vol. 42. – № 8. – P. 1069–1075. Krinulović K.S., Vasić V.M. Interaction of some Pd(II) complexes with Na+/K+ ATPase: Inhibition, kinetics, prevention and recovery // Journal of Enzyme Inhibition and Medicinal Chemistry. – 2006. – Vol. 21. – № 4. – P. 459–465.Sakakibara N., Suzuki K., Kaneta H., Yoshimura Y., Deyama Y., Matsumoto A., Fukuda H. Inhibition of Na+,K+ ATPase by cisplatin and its recovery by 2 mercaptoethanol in human squamous cell carcinoma cells // Anticancer Drugs. – 1999. – Vol. 10. – № 2. – P. 203–211.Tatyanenko L.V., Kotelnikova R.A., Zakharova I.A., Moshkovskii Yu.Sh. On the Mechanism of Platinumand Palladium-Albumin Complexes Interaction with (Ca2+ Mg2+) dependent ATP ase of Sarcoplasmic Reticulum of Skeletal Muscles // Inorganica Chimica Acta. – 1981. – Vol. 56. – P. 89–93.Рапопорт Ж.Ж. Промышленная аллергия и токсикоз (платиноз). – Красноярским гос. мед. ин-т. Красноярск : [б. и.], 1976. – 118 с.
Татьяненко Л.В., Соколова Н.В., Мошковский Ю.Ш. Сравнительное исследование механизма действия биологически активных соединений на мембраносвязывающую митохондриальную моноаминоксидазу и Ca2+, Mg2+ зависимую АТФ азу саркоплазматического ретикулума // Вопросы медицинской химии. – 1982. – Т. 28. – № 6. – С. 126–131.Hong R., Li X. Discovery of monoamine oxidase inhibitors by medicinal chemistry approaches // Medicinal Chemistry Communications. – 2019. – Vol. 10. – № 1. – P. 10–25.Chiuccariello L., Houle S., Miller L., Cooke R.G., Rusjan P.M., Rajkowska G., Levitan R.D., Kish S.J., Kolla N.J., Ou X., Wilson A.A., Meyer J.H. Elevated Monoamine Oxidase A Binding During Major Depressive Episodes Is Associated with Greater Severity and Reversed Neurovegetative Symptoms // Neuropsychopharmacology. – 2014. – Vol. 39. – P. 973–980.Денисов М.С., Дмитриев М.В., Ерошенко Д.В., Слепухин П.А., Шавкунов С.П., Глушков В.А. Катионно-анионные комплексы PdII с катионом адамантилимидазолия: синтез, структурные исследования и МАО ингибирующая активность // Журнал неорганической химии. – 2019. – Т. 64. – № 1. – С. 38–50. Albert J., Cadena J.M., González A., Granell J., Solans X., Font-Bardia M. The first NH aldimineorganometallic compound. Isolation and crystal structure // Chemical Communications. – 2003. – Vol. 41. – № 4. – P. 528–529.Petrović Z.D., Hadjipavlou-Litina D., Pontiki E., Simijonović D., Petrović V.P. Diethanolamine Pd(II) complexes in bioorganic modeling as model systems of metallopeptidases and soybean lipoxygenase inhibitors // Bioorganic Chemistry. – 2009. Vol. 37. – № 5. – P. 162–166. Ylä-Herttuala S., Rosenfeld E.M., Parthasarathy S., Glass K.C., Sigal E., Witztum L.J., Steinberg D. Colocalization of 15 lipoxygenase mRNA and protein with epitopes of oxidized low density lipoprotein in macrophage rich areas of atherosclerotic lesions // Proceedings of the National Academy of Sciences of the United States of America. – 1990. – Vol. 87 – № 18. – P. 6959–6963.Shultz M.D., Lassig J.P., Gooch M.G. Palladium – a new inhibitor of cellulose activities // Biochemical and biophysical research communications. – 1995. – Vol. 209. – № 3. – P. 1046–1052.Lassig J.P., Shultz M.D., Gooch M.G., Evans B.R., Woodward J. Inhibition of Cellobiohydrolase I from Trichoderma reesei by Palladium // Archives of Biochemistry and Biophysics. – 1995. – Vol. 322. – № 1. – P. 119–126.Abu-Surrah A.S. Development and Current Status of Unconventional Platinum Anticancer Complexes // Mini Reviews in Medicinal Chemistry. – 2007 – Vol.7. – № 2. – P. 203 211.Nolan S.P. N-Heterocyclic Carbenes Effective Tool for Organometallic Synthesis. – Wiley vch Verlag GmbH & Co. KGaA, 2014. – 543 p. Erdemir F., Celepci D.B., Aktaş A., Gök Ye., Kaya R., Taslimi P., Demir Ye., Gulçin İ. Novel 2 aminopyridine liganded Pd(II) N heterocyclic carbene complexes: Synthesis, characterization, crystal structure and bioactivity properties // Bioorganic Chemistry. – 2019. – Vol. 91. – P. 103134–103135.Aktaş A., Celepci D.B., Kaya R., Taslimi P., Gök Y., Aygün M., Gülçin İ. Novel morpholine liganded Pd-based N-heterocyclic carbene complexes: Synthesis, characterization, crystal structure, antidiabetic
and anticholinergic properties // Polyhedron. – 2019. – Vol. 159. – P. 345–354. Bal S., Demirci Ö., Şen B., Taslimi P., Aktaş A., Gök Ye., Aygün M., Gülçin İ. PEPPSI type Pd(II)NHC complexes bearing chloro /fluorobenzyl group: Synthesis, characterization, crystal structures, α glycosidase and acetylcholinesterase inhibitory properties // Polyhedron. – 2021. – Vol. 198 – P. 115060–115067.Hansen R.A., Gartlehner G., Webb A.P., Morgan LC., Moore CG., Jonas D.E. Efficacy and safety of
donepezil, galantamine, and rivastigmine for the treatment of Alzheimer’s disease: A systematic review and meta analysis // Clinical Interventions in Aging. – 2008. – Vol. 3. – № 2. – P. 211–225.Karataş M.O., Çalgın G., Alıcı B., Gökçe B., Gençer N., Tok T.T., Arslan O., Kılıç‐Cıkla I., Özdemir N. Inhibition of paraoxonase 1 by coumarin‐substituted N‐heterocyclic carbene silver(I), ruthenium(II) and palladium(II) complexes // Applied Organometallic Chemistry. – 2019. – Vol. 33. – № 10. – P. e5130.
Wu J., Fang M., Zhou X., Zhu B., Yang Z. Paraoxonase 1 gene polymorphisms are associated with an increased risk of breast cancer in a population of Chinese women. // Oncotarget. – 2017. – Vol. 8. – № 15. – P. 25362–25371.Asma M., Badshah A., Ali S., Sohail M., Fettouhi M., Ahmad S., Malik A. Synthesis, Characterization of Mixed Ligand Palladium(II) Complexes of Triphenylphosphine and Anilines and their Enzyme Inhibition Studies against β glucuronidase. The Crystal Structure of trans dichloro (m chloroaniline) (triphenylphosphine)palladium(II) // Transition Metal Chemistry. – 2006. – Vol. 31. – P. 556–559. Nyhan W.L., Barshop B., Ozand P. Atlas of metabolic diseases second edition. – London, UK: Hodder
Arnold, 2005. – 788 p.Chen Ch., Sun L. Yu., Gao H., Kang P. W., Li J. Q., Zhen J. B., Ke Wu Yang K.-W. Identification of
Cisplatin and Palladium(II) Complexes as Potent Metallo β lactamase Inhibitors for Targeting Carbapenem Resistant Enterobacteriaceae // ACS Infectious Diseases. – 2020. – Vol. 6 – № 5. – P. 975−985.Qurrat ul Ain, Ashiq U., Jamal R.A., Saleem M., Mahroof Tahir M. Alpha glucosidase and carbonic anhydrase inhibition studies of Pd(II) hydrazide complexes // Arabian Journal of Chemistry – 2017. – Vol. 10. – № 4. – P. 488–499.Petrović Z.D., Djuran M.I., Heinemann F.W., Rajković S., Trifunović S.R. Synthesis, structure, and hydrolytic reaction of trans dichlorobis(diethanolamine N)palladium(II) with N acetylated L histidylglycine dipeptide // Bioorganic Chemistry. – 2006. – Vol. 34. – № 5. – P. 225–234. Mital R., Shah G.M., Srivastava T.S., Bhattacharya R.K. The effect of some new platinum (II) and palladium (II) coordination complexes on rat hepatic nuclear transcription in vitro // Life Sciences. – 1992. – Vol. 50. – № 11. – P. 781–790. Денисов М.С., Гагарских О.Н., Утушкина Т.А. Пиридиниминовые комплексы палладия (II): синтез и ингибирование моноаминоксидазы // Вестник Пермского университета. Сер. «Химия». – 2021. – Т. 11 – № 1. – С. 30–58.Dilek E., Caglar S., Erdogan K., Caglar B., Sahin O. Synthesis and characterization of four novel palladium(II) and platinum(II) complexes with 1 (2 aminoethyl)pyrrolidine, diclofenac and mefenamic acid: In vitro effect of these complexes on human serum paraoxanase1 activity // Journal of
Biochemical and Molecular Toxicology. – 2018. – Vol. 32. – № 4. – P. e22043.Krinulović K., Bugarčić Ž., Vrvić M., Krstić D., Vasić V. Prevention and recovery of (μ3 diethylentriamino) chloro palladium(II) chloride induced inhibition of Na/K¬ATPase by SH containing ligands – l cysteine and glutathione // Toxicology in Vitro. – 2006. – Vol. 20. – № 8. – P. 1292–1299.Hegazy W.H., Al Faiyz Ya.S. Synthesis, characterization, and antitumor activities of 1,1′-diacetylferrocene dihydrazone containing phenolic group and its complexes with Pd(II) and Pt(II) // Medicinal Chemistry Research. – 2014. – Vol. 23. – № 1. – P. 518–525.
Lima M.A., Costa V.A., Franco M.A., de Oliveira G.P., Deflon V.M., Rocha F.V. Palladium(II) complexes bearing thiosemicarbazone and phosphines as inhibitors of DNA Topoisomerase II enzyme: Synthesis, characterizations and biological studies // Inorganic Chemistry Communications. – 2020. – Vol. 112. – P. 107708. Fry A.M., Chresta C.M., Davies S.M., Walker M.C., Harris A.L., Hartley J.A., Masters J.R.W., Hickson I.D. Relationship between topoisomerase II level and chemosensitivity in human tumor cell lines // Cancer Research. – 1991. – Vol.51. – № 24. – P. 6592–6595. Gama N.H., Elkhadir A.Y.F., Gordhan B.G., Kana B.D., Darkwa J., Meyer D. Activity of phosphino palladium(II) and platinum(II) complexes against HIV 1 and Mycobacterium tuberculosis // Biometals. – 2016. – Vol. 29. – P. 637–650.Рахимова А.В., Салаватович А.Н., Анварович З.Р., Габдурахманов И.А., Валиулловна К.Р., Меметович Дж.У. Патент РФ № 2709512 от 14.02.2019 г.Parrilha G.L., Ferraz K.S.O., Lessa J.A., Oliveira K.N., Rodrigues B.L., Ramos J.P., Souza-Fagundes E.M., Ott I., Beraldo H. Metal complexes with 2 acetylpyridine N(4) orthochlorophenylthiosemicarbazone: Cytotoxicity and effect on the enzymatic activity of thioredoxin reductase and glutathione reductase // European Journal of Medicinal Chemistry. – 2014. – Vol. 84. – № 12. – P. 537-544.Becker K., Gromer S., Schirmer R.H., Müller S. Thioredoxin reductase as a pathophysiological factor and drug target // European Journal of Biochemistry. – 2000. – Vol. 267. – № 20. – P. 6118–6125. Ott I. On the medicinal chemistry of gold complexes as anticancer drugs // Coordination Chemistry Reviews. – 2009. – Vol. 253. – № 11 12. – P. 1670–1681. Vieites M. , Smircich P., Parajón Costa B., Rodríguez J., Galaz V., Olea Azar C., Otero L., Aguirre G., Cerecetto H., González M., Gómez-Barrio A., Garat B., Gambino D. Potent in vitro anti Trypanosoma cruzi activity of pyridine 2 thiol N oxide metal complexes having an inhibitory effect on parasite-specific fumarate reductase // JBIC Journal of Biological Inorganic Chemistry. – 2008. – Vol. 13. – № 5. – P. 723–735.Carneiro Z.A., Lima J.C., Lopes C.D.,Gaspari A.P.S., Albuquerque S., Dinelli L.R., Veloso Silva L.L.W., Paganelli M.O., Libardi S.H., Oliveira C.G., Deflon V.M., Oliveira R.J., Borges J.C., Maia P.I.S. Heterobimetallic nickel(II) and palladium(II) complexes derived from S benzyl N (ferrocenyl) methylenedithiocarbazate: Trypanocidal activity and interaction with Trypanosoma cruzi Old Yellow Enzyme (TcOYE) // European Journal of Medicinal Chemistry. – 2019. – Vol. 180. – № 15. – P. 213–223. Fricker S.P., Mosi R.M., Cameron B.R., Baird I., Zhu Yo., Anastassov V., Cox J., Doyle P.S., Hansell E., Lau G., Langille J., Olsen M., Qin L., Skerlj R., Wong R.S.Y., Santucci Z., McKerrow J.H. Metal compounds for the treatment of parasitic diseases // Journal of Inorganic Biochemistry. – 2008. – Vol. 102. – № 10. – P. 1839–1845.Buldurun K., Turan N., Bursal E., Aras A., Mantarcı A., Çolak N., Türkan F., Gülçin İ. Synthesis, characterization, powder X ray diffraction analysis, thermal stability, antioxidant properties and enzyme inhibitions of M(II) Schiff base ligand complexes // Journal of Biomolecular Structure and
Dynamics. – 2020. – Doi: 10.1080/07391102.2020.1802340.Şahin Ö, Özdemir Ü.Ö., Seferoğlu N., Adem Ş., Seferoğlu Z. Synthesis, characterization, molecular docking and in vitro screening of new metal complexes with coumarin Schiff base as anticholine esterase and antipancreatic cholesterol esterase agents // Journal of Biomolecular Structure and Dynamics. – 2021. Doi: 10.1080/07391102.2020.1858163.Türkan F., Huyut Z., Atalar M.N. The toxicological impact of some avermectins on human erythrocytes glutathione S transferase enzyme // Journal of Biochemical and Molecular Toxicology. – 2018. – Vol. 32. – № 10. – P. e22205.Alyar S., Şen C., Alyar H., Adem Ş., Kalkanci A., Ozdemir U.O. Synthesis, characterization, antimicrobial activity, carbonic anhydrase enzyme inhibitor effects, and computational studies on new Schiff bases of Sulfa drugs and their Pd(II), Cu(II) complexes // Journal of Molecular Structure. – 2018. – Vol. 1171. – № 5. – P. 214–222.Özbek N., Alyar S., Memmi B.K., Gündüzalp A.B., Bahçeci Z., Alyar H. Synthesis, characterization, computational studies, antimicrobial activities and carbonic anhydrase inhibitor effects of 2 hydroxyacetophenone N methyl p toluenesulfonylhydrazone and its Co(II), Pd(II), Pt(II) complexes // Journal of Molecular Structure – 2017. – Vol. 1127. – P. 437–448.Milenković D.A., Dimić D.S., Avdovićac E.H., Marković Z.S. Several coumarin derivatives and their Pd(II) complexes as potential inhibitors of the main protease of SARS CoV 2, an in silico approach // RSC Advances. – 2020. – Vol. 2020. – № 58. – P. 35099–35108.