RU2641112C2 - Acyl derivative of aminophenol as type a monoamine oxidase activator - Google Patents
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Abstract
Description
Изобретение относится к экспериментальной биологии, медицине, биохимии и касается фармакологически активного производного аминофенола - 2(N-ацетилацетамидо)фенил ацетатаThe invention relates to experimental biology, medicine, biochemistry and relates to a pharmacologically active derivative of aminophenol - 2 (N-acetylacetamido) phenyl acetate
Вышеуказанное соединение, синтезированное химическим путем, может найти применение в медицинской биохимии при изучении свойств различных моноаминоксидаз и в медицине в качестве активатора этих ферментов, а также в изучении развития онкологических процессов, как на уровне роста опухоли, так и при коррекции психического статуса больных [1-3].The above compound, synthesized chemically, can be used in medical biochemistry in the study of the properties of various monoamine oxidases and in medicine as an activator of these enzymes, as well as in the study of the development of oncological processes, both at the level of tumor growth and in the correction of the mental status of patients [1 -3].
Моноаминоксидазы (МАО) - ключевые ферменты катаболизма биогенных аминов, принимающих участие в передаче нервных импульсов в центральной нервной системе и на периферии.Monoamine oxidases (MAOs) are the key enzymes of the catabolism of biogenic amines involved in the transmission of nerve impulses in the central nervous system and on the periphery.
Различают два изофермента МАО - типа А и типа Б. Они на 70% идентичны по аминокислотному составу, имеют около 60 кДа веса на одну субъединицу и состоят, за редким исключением, из двух субъединиц. Эти формы кодируются различными генами, различаются относительной чувствительностью к специфическим ингибиторам и характеризуются перекрывающейся субстратной специфичностью. Предполагаются различные физиологические функции для МАО типа А и Б. Считается, что повышающаяся в течение жизни активность МАО типа Б (субстраты - дофамин, тирамин, фенилэтиламин) связана с нейродегенеративными процессами (болезни Паркинсона и Альцгеймера). Активность МАО типа А (субстраты - серотонин, норадреналин, тирамин) стабильна в течение жизни и связана со способностью к обучению и серьезным патологическим поведенческим нарушениям.Two MAO isoenzymes are distinguished - type A and type B. They are 70% identical in amino acid composition, have about 60 kDa weight per subunit and consist, with rare exceptions, of two subunits. These forms are encoded by various genes, differ in relative sensitivity to specific inhibitors, and are characterized by overlapping substrate specificity. Various physiological functions for MAO type A and B are assumed. It is believed that the activity of MAO type B increasing during life (substrates dopamine, tyramine, phenylethylamine) is associated with neurodegenerative processes (Parkinson's and Alzheimer's disease). The activity of MAO type A (substrates - serotonin, norepinephrine, tyramine) is stable throughout life and is associated with learning ability and serious pathological behavioral disorders.
Применяемые в медицине при нарушениях активности аминоксидаз лекарственные препараты относятся к различным классам: бензодиазепинам, блокаторам кальциевых каналов, антиэпилептикам, антипсихотикам, обратимым ингибиторам МАО типа А и В. В терапии используют также необратимые ингибиторы МАО, хотя эти соединения опасны, поскольку вызывают «сырный синдром». Все вышеперечисленные соединения не универсальны для больных, их комбинация представляется полезной, но требует дополнительного изучения [4, 5].Medicines used in medicine for disorders of aminoxidase activity belong to different classes: benzodiazepines, calcium channel blockers, antiepileptics, antipsychotics, reversible MAO inhibitors of type A and B. In therapy, irreversible MAO inhibitors are also used, although these compounds are dangerous because they cause "cheese syndrome" ". All of the above compounds are not universal for patients, their combination seems useful, but requires additional study [4, 5].
Предлагаемое в данной заявке соединение позволяет непосредственно воздействовать на сниженную при некоторых заболеваниях активность МАО типа А. Известно, что сниженная активность этой формы фермента наблюдается у людей при депрессивных состояниях, мании, суициде, асоциальном поведении, увеличенной уязвимости к стрессу при умственных проблемах у детей [6]. Данные по наличию активаторов моноаминоксидаз в литературе отсутствуют.The compound proposed in this application allows you to directly affect the reduced activity of MAO type A in certain diseases. It is known that the reduced activity of this form of the enzyme is observed in people with depressive states, mania, suicide, antisocial behavior, increased vulnerability to stress in children with mental problems [ 6]. There are no data on the presence of monoamine oxidase activators in the literature.
Исследования свойств предлагаемого соединения были проведены на препаратах митохондрий мозга быка и печени крысы. Для их получения использовали 10% гомогенаты ткани. Выделение из печени крыс проводилось в 0,02 М фосфатном буфере, содержащем 0,005 М этилендиаминтетраацетат и 0,25 М сахарозу. Осадок, полученный при центрифугировании препаратов при 800 g в течение 10 мин, отбрасывали. Митохондрии получали после центрифугирования надосадочной жидкости при 8500 g в течение 30 мин и двухкратной промывки 0,02 М фосфатным буфером.Studies of the properties of the proposed compounds were conducted on preparations of mitochondria of the brain of a bovine and rat liver. To obtain them, 10% tissue homogenates were used. Isolation from rat liver was carried out in 0.02 M phosphate buffer containing 0.005 M ethylenediaminetetraacetate and 0.25 M sucrose. The precipitate obtained by centrifuging the preparations at 800 g for 10 min was discarded. Mitochondria were obtained after centrifugation of the supernatant at 8500 g for 30 min and washing twice with 0.02 M phosphate buffer.
Выделение из стволовой части мозга быка проводилось в 0,25 М растворе сахарозы последовательной промывкой митохондрий 0,125 М сахарозой, водой и 0,05 М фосфатным буфером при pH 7,6. Центрифугирование проводили в вышеописанных условиях.Isolation from the brain stem of a bull was carried out in a 0.25 M sucrose solution by successive washing of mitochondria with 0.125 M sucrose, water and 0.05 M phosphate buffer at pH 7.6. Centrifugation was carried out under the above conditions.
Белок определяли по методу Лоури. Активность полученных препаратов определяли:Protein was determined by the Lowry method. The activity of the obtained preparations was determined:
1) микродиффузионным методом при концентрации субстратов: серотонина - 10-3 М, тирамина - 3,2×10-3 М, фенилэтиламина - 0,8×10-3 М;1) microdiffusion method at a concentration of substrates: serotonin - 10 -3 M, tyramine - 3.2 × 10 -3 M, phenylethylamine - 0.8 × 10 -3 M;
2) радиометрическим методом при концентрации субстратов: серотонина - 10-4 М, тирамина - 10-4 М, фенилэтиламина - 0,5×10-4 М [4];2) by radiometric method at a concentration of substrates: serotonin - 10 -4 M, tyramine - 10 -4 M, phenylethylamine - 0.5 × 10 -4 M [4];
3) спектрофотометрическим методом по образованию семикарбазона при концентрации серотонина - 0,54×10-4 М [7];3) spectrophotometric method for the formation of semicarbazone at a concentration of serotonin - 0.54 × 10 -4 M [7];
4) спектрофотометрическим методом по образованию продукта с хромогенной смесью при концентрации тирамина 6×10-4 М [8];4) spectrophotometric method for the formation of a product with a chromogenic mixture at a tyramine concentration of 6 × 10 -4 M [8];
5) спектрофотометрическим методом по образованию бензальдегида при концентрации бензиламина (БА) 6×10-3 М [9].5) spectrophotometric method for the formation of benzaldehyde at a concentration of benzylamine (BA) 6 × 10 -3 M [9].
Результаты исследования действия производного аминофенола-2(N-ацетиламидо)фенил ацетата на серотониндезаминазную активность МАО из мозга представлены на фиг. 1-3.The results of a study of the effect of the aminophenol-2 (N-acetylamido) phenyl acetate derivative on the serotonin deaminase activity of MAO from the brain are shown in FIG. 1-3.
На фиг. 1 представлено изменение активности МАО А в зависимости от концентрации аминофенола. Результаты свидетельствуют о том, что при низких концентрациях исследуемого соединения наблюдается активация на 20-60%. При дальнейшем увеличении концентрации активатора наблюдается торможение активности МАО типа А.In FIG. Figure 1 shows the change in MAO A activity as a function of the concentration of aminophenol. The results indicate that at low concentrations of the test compound, activation is observed at 20-60%. With a further increase in the activator concentration, inhibition of MAO type A activity is observed.
На фиг. 2 представлена зависимость активности моноаминоксидазы Б от концентрации аминофенола. Как следует из представленных данных, в исследуемых концентрациях МАО типа Б активации не подвергается.In FIG. 2 shows the dependence of the activity of monoamine oxidase B on the concentration of aminophenol. As follows from the data presented, in the studied concentrations of MAO type B is not exposed to activation.
Полученные результаты свидетельствуют об активации именно МАО типа А (избирательный субстрат - серотонин), а не МАО типа Б (субстрат - бензиламин). Высокие концентрации вещества вызывают неспецифическую инактивацию ферментов. Выявленное действие предлагаемого в качестве активатора соединения является обратимым, т.к. разведение заингибированного фермента приводит к восстановлению его активности.The results obtained indicate the activation of MAO type A (selective substrate - serotonin), and not MAO type B (substrate - benzylamine). High concentrations of the substance cause nonspecific inactivation of the enzymes. The revealed action of the compound proposed as an activator is reversible, because dilution of the inhibited enzyme leads to the restoration of its activity.
Тип торможения или активации катализируемой МАО реакции определен с использованием метода двойных обратных величин по Лайнуиверу-Берку и представлен на фиг. 3.The type of inhibition or activation of the MAO-catalyzed reaction is determined using the Lineweaver-Burke double return method and is shown in FIG. 3.
Из представленных данных видно, что изучаемое соединение влияет как на сродство фермента к субстрату, так и на скорость каталитического распада, т.е. выявлен смешанный характер активации-торможения.It can be seen from the presented data that the studied compound affects both the affinity of the enzyme for the substrate and the catalytic decomposition rate, i.e. revealed a mixed nature of activation-inhibition.
ЛИТЕРАТУРАLITERATURE
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6. Chajkowski-Scarry S, Rimoldi JM. Future Med Chem. Monoamine oxidase A and В substrates: probing the pathway for drug development. 2014, 6 (6), 697-717.6. Chajkowski-Scarry S, Rimoldi JM. Future Med Chem. Monoamine oxidase A and B substrates: probing the pathway for drug development. 2014, 6 (6), 697-717.
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8. Holt A., Sharman D.F., Baker G.B. A continuous spectrophotometric assay for monoamine oxidase and related enzymes in tissue homogenates. Palcic MMA nal Biochem. 1997, 244 (2), 384-92.8. Holt A., Sharman D.F., Baker G. B. A continuous spectrophotometric assay for monoamine oxidase and related enzymes in tissue homogenates. Palcic MMA nal Biochem. 1997, 244 (2), 384-92.
9. Т.А. Москвитина, Н.И. Соловьева. Физиологическое значение аминоксидаз и методы определения их активности. Клиническая и лабораторная диагностика, 2011, 2, 3-7.9. T.A. Moskvitina, N.I. Solovyov. The physiological significance of aminoxidases and methods for determining their activity. Clinical and laboratory diagnostics, 2011, 2, 3-7.
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| RU2641112C2 true RU2641112C2 (en) | 2018-01-16 |
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| RU2015155068A RU2641112C2 (en) | 2015-12-23 | 2015-12-23 | Acyl derivative of aminophenol as type a monoamine oxidase activator |
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Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SU1578125A1 (en) * | 1988-02-11 | 1990-07-15 | Тюменский государственный университет | Inhibitor of monoaminooxidase ferment |
| SU1114021A1 (en) * | 1982-11-11 | 1995-12-20 | Институт Тонкой Органической Химии Им.А.Л.Мнджояна | 4-methoxibenzylguanidine or its sulfate |
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SU1114021A1 (en) * | 1982-11-11 | 1995-12-20 | Институт Тонкой Органической Химии Им.А.Л.Мнджояна | 4-methoxibenzylguanidine or its sulfate |
| SU1578125A1 (en) * | 1988-02-11 | 1990-07-15 | Тюменский государственный университет | Inhibitor of monoaminooxidase ferment |
Non-Patent Citations (3)
| Title |
|---|
| B. WITKOP et al. Acid- and Base-catalyzed Rearrangements of a Ring-Chain Tautomeric Ozonide, J. AMER. CHEM. SOC., 1952, vol. 74, pp. 3861-3866. * |
| H. GERSHON et al. Reexamination of the Thermolytic Rearrangement of 4-Halophenyl Azides to 2-Aminophenols and other Products, MONATSHEFTE FUR CHEMIE, 1993, 124(4), pp. 367-379. * |
| H. GERSHON et al. Reexamination of the Thermolytic Rearrangement of 4-Halophenyl Azides to 2-Aminophenols and other Products, MONATSHEFTE FUR CHEMIE, 1993, 124(4), pp. 367-379. B. WITKOP et al. Acid- and Base-catalyzed Rearrangements of a Ring-Chain Tautomeric Ozonide, J. AMER. CHEM. SOC., 1952, vol. 74, pp. 3861-3866. * |
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