Биотехнологическое получение стабильно-меченых препаратов антибиотика семейства зервамицина из Emericellopsis salmosynnemata
Диссертация
Чтобы получить более полную информацию о механизме каналообразования данного антибиотика, необходимо изучить его структуру и динамику при ассоциировании с фосфолипидными мембранами. Для проведения подобных исследований используют препараты, меченные стабильными изотопами. Данная работа посвящена разработке биотехнологического метода получения тотально-меченых препаратов зервамицина IIB. К этому… Читать ещё >
Список литературы
- Харкевич Д.А. Фармакология.// М.: Медицина, 1993.
- Франклин Т. Биохимия антимикробного действия.// М.: Мир. 1984.
- Waksman S., Woodruff Н. A new antibiotoc actinomicine prodUsed by Streptomyces sp. //Proc. Soc. Exp. Biol. Med. 1940. v.45 p.609−614.
- Eagle H., Foley G. Actinomicine D: Investigations of biological activities. //Cancer Res. 1958. v.18. p.1017−1021.
- Планельес X.X. Аурантин противоопухолевый антибиотический препарат из группы актиномицинов. // М.: Мир. 1962.
- Терентьева Т.Г. Противоопухолевая активность препаратов группы актиномицина. .//Хим.-Фармацевт. Журн. 1977. т.11. с.143−146.
- Frei Е. Anticancer activity of actinomicine D. .//Chemother. Rep. 1974. V.58 part I. p. 4954.
- Hotchkiss R.D., Dubos R.J. Antibacterial compound from Вас. Brevis. .//J. Biol. Chem. 1940. V.132.
- Гаузе Г. Ф. Грамицидин С и его применение. // М., 1952.
- Кожибски Т., Ковшик-Гиндифер 3. Антибиотики, происхождение, природа, свойства. //Варшава, T. I, Т.2,1969.
- Gross Е., Morell J.L. Structure of peptide antibiotic nisine. //J. Amer. Chem. Soc. 1970. V.92. p.2919
- Charney J., Fisher W.P. et al. Peptidolactones, structure and properties. //Antibiot. And Chemother. 1953 v.3 p. 1285
- Bartz Q.R., Standiford J. et al. Antibacterial ativities of peptidolactones. //Antibiot. Ann. 1954−1955. p.777.
- Sheehan J.C., Mania D., Nakamura S. et al. Structure and properties of antibiotics peptidolactones. //J. Amer. Chem. Soc. 1968. V.90. p.462.
- Шемякин M.M., Хохлов A.C., Колосов M.H. и др. Химия антибиотиков. //М., 1961
- Maeda К., Kosaka Н., Yagishita К. et al. Asaserine, a new antitumor antibiotic. //J. Antibiot. 1956. V.9. p.82−85.
- McCormick M.H., Stark W.M. et al. Structure elucidation of new antibiotic netropsine. //Antibiot. Ann. 1955−1956. p.606−611.
- Aoyagi T. et.al. Poststatin, a new inhibitor of prolylendopeptidase. //J.Antibiot. 1991. V.44(9) p.949−955.
- Woo J.T. et al. Cathestatins, new cysteine protease inhibitors prodused by Penicillium ctrinum. //Biosci. Biotech. Biochem., 1995. v.59(2). p.350−352.
- Hagano Y., Takeuchi N. et. al. Improved production of phenomycin by a Genetically Engineered Escherichia coli. //J. Antibiot. 1996. Vol.49(I). p.81−85.
- Chatterjee S. et al. Mersacidin, a novel antibiotic from Baciilus. //J. Antibiot. 1992. V.45(6). p.832−838.
- Komiyama S., Omoguro S. et al. A new antibiotic cypemicin. //J. Antibiot. 1993. V.46(ll). p.166−171
- Егоров H.C. Антибиотики полипептиды. //M., 1987
- Grafe U., Ihn W. et al. Helioferins- novel antifungal lipopeptides from Mucogone rosea. //J. Antbiot. 1995. v.48(2). p. 126−133.
- Kumazava S. et al. Structural elucidation of aibellin, a new peptide antibiotic. //J. Antibiotic. 1994. V.47(10). p. l 136−1144.
- Chikanihi T. et al. Clonostachin line tetradecapeptide antibiotic. //J. Antibiotic. 1997. V.50(2). p. 105−110.
- Kalmokoff M.L., Lu D, Witford M.F. Evidence for production of a new lantibiotic (butyrivibroicin OR79A) by Butyrivibreo Jibrisolvens OR79. //Appl. Environ. Microbiol. 1999. V.65(5). p.2128−2135.
- Shimanaka K. et al. Novel antibiotics amithiamicins. //J. Antibiot. 1994. V.47(6). p.668−674.
- Bong-Sik Yun et al. Genintiocin, a novel thiopeptide produced by Streptomices sp. DD84. //J. Antibiot. 1994. V.47(9). p.969−975.
- Bong-Sik Yun et al. Promotiocins A and B, novel tiopeptides with A typA promoter inducing activity produced by Streptomices sp. SF2741. IIJ. Antibiot. 1994. V.47(4). p.510−514.
- Carnio M.C. et al. The macricyclic peptide antibiotic mocrococcin P (I) is secreted by the food-born bacterium staphilococcus equorum WS 2733. //App. Environ. Microbiol. 2000. V.66(6). 2378−2384.
- Selva E. et al. Antibiotics A21459 A and B, new inhibitors of bacterial protein synthesis. J. Antibiot. 1996. Vol.49(2). p.145−148.
- Blond A., Peduzzi J. The cyclic structure of microcin J25. //Eur.J.Biochem. 1999. V.259(3). P.747−755.
- Quarta C. et al. Isolation and structure detrmination of a novel complex of the teicoplanin family. //J.Antibiot. 1996. V.49(6). p.644−650.
- Vertesy L. et al. New 4-oxovancosamine-containing glycopeptide antibiotics from Amycolatopsis sp. Y-86,21 022. //J.Antib. 1996. V.49(l). p.115−117.
- Borghi A. et al. Deacylation of the glycopeptide antibiotic A40926 by Actinoplanes teichomiceticus ATCC 31 121. //J.Antib. 1996. V.49(6). p.607−608.
- Tanaka H. et al. A new antibiotic amphamicine. //Biochem. Biophis. Res. Comm. 1979. V.86. p.902.
- Inoue T. et al. Isolation of plactins A, B, C and D, novel cyclic polypeptides. //J.Antib. 1996. V.49(l). p.45−49.
- Ogava T. et al. Res-701−2, -3 and -4, novel and selective endothelin type b receptor antagonist produced by Streptomices sp. //J.Antib. 1995. V.48(ll). p.1213−1215.
- Nakamura M. et al. Stachibocins, novel endothelin receptor antagonists. //J.Antib. 1995. V.48(12). p.1389−1395.
- Sahl H.G. et al. Voltage-dependent depolarization of bacterial membranes by the peptide antibiotic nisin. //Arch. Microbiol. 1987. V.149(2). p.120−124.
- Gao F.H. et al. Mechanism of action of the peptide antibiotic nisin in liposomes. //Appl. Environ. Microbiol. 1991. V.57(8). p.2164−2170.
- Chan W.C. et al. Structure-activity relationship in the peptide antibiotic nisin- role of dehydroalanine-5. //Appl. Environ. Microbiol. 1996. V.62(8). P.2966−2969.
- Hasumi K. et al. Inhibition of Acyl-Co: cholesterol acyltransferase by isohalobacyllin. //J.Antibiot. 1995. V.48(12). p.1419−1424.
- Hochlowski J.E. et al. Aselacins, novel compounds that inhibit binding of endothelin to its receptor. //J.Antibiot. 1994. V.47(5). p.528−535.
- Morino T. et al. Stevastelins, novel immunosuppressants produced by Penicilinum. //J.Antibiot. 1994. V.47(ll). p.1341−1343.
- Yoshikawa Y. et al. Isolation, structures and antifungal activities of new aureobasidins. //J.Antibiot. 1993. V.46(9). p.1347−1354.
- Kimomyo A. Use of a-aminoisobutyric acid and isovalin as marker aminoacids for the detection of fungal polypeptied antibiotics. /Dissertation Н98−494/. //Japan. 1997.
- Becker D. Protein mass spectrometry: application to analitical boitechnology. /Dissertation H97−162/.//Germany. 1996.
- Tomio Morino et al. Structural Determination of Stevastelins, Novel Decipeptides from Penicillium sp. //J.Antibiot. 1996. V.49(6). p.564−572.
- John E. Leet et al. Himistatin, a new Antitumor Antibiotics from Streptomices hygroscopicopicus. //J.Antibiot. 1996. V.49(3). p.299−304.
- E. Попов и др. Проблема белка. //М. Наука. 1996. Т.2.
- Rodriguez М. J. et al. Relationship between Structure and Biological Activity of Novel R 106 Analogs. //J.Antibiot. 1996. V.49(4). p.386−389.
- Yosikava Y. et al. Isolation, structure and antifunginal activities of new aureubasidins. //J.Antibiot. 1996. V.49. p.1347−1354
- Takesako К et al. Preparation of antibacterial antibiotic R 106. //патент JP 3 044 398, 1989.
- Takesako К et al. Biological properties of aureobasidin A. //J.Antibiot. 1993. У.46. p. 1414−1420.
- Lociuro S. et al. Antimicrobial activity of chemically mondified thiazol peptide antibiotic GE2270A. //J.Antibiot. 1997. V.50(4). p.344−349.
- Heffron S.E., Jurnak F. Structure of an EF-Tu complex with thiazol peptide antibiotic determined at 2.35 A resolution. //Biochemistry. 2000. 39(1) p.37−45.
- A.Y.Pavlov et al. Carboxamides and hidraside of glycopeptide antibiotic eremomicin. //J.Antibiot. 1996. V.49(2). p.194−198.
- Hermann R. et al. Synthesis and antibacterial activity of derivtives of the glycopeptide antibiotic A-40 926 and its aglycone. //J.Antibiot. 1996. V.49(12). p. 1236−1239.
- Cooper R.D.G. et al. Reductive alkylation of glycopeptide antibiotics. //J.Antibiot. 1996. V.49(6). p.575−581.
- Chamoney W.S. Reductive methods for isotopic labeling of antibiotics. //An. Biochem. 1989. V.181 p.90−95.
- Breukink E. et al. Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic. //Science 1999, Dec 17,286(5448): 2361−2364.
- Grdadolnik S.G. Mierke D.F. Structural characterization of the molecular dimer of the peptide antibiotic vancomycin. //J. Chem. Inf. Comput. Sci. 1997. Nov-Dec- 37(6): 10 441 047.
- Linsdell H. et al. Dimerization of A82846B, Vancomycin and Ristocetin. //J.Antibiot. 1996. V.49(2). p.181−186.
- Tsuda M. et al. Stereospecific synthesis of a novel protein transferase inhibitor, valinoctinA and its analogues. //J.Antibiot. 1996. V.49(10). p.1031−1035.
- Tsitsumi S. et al. Syntesis and structure-activity relationship of peptydil alfa-keto heterocycles as novel inhibitors of prolyl endopeptidase. //J.Med. Chem. 1994, 37(21):3492−3502.
- Tsuda M. et al. Poststatin: N-cycloalkylamide analogues. //J.Antibiot. 1996. V.49(9). p.909−911.
- Tsuda M. et al. Poststatin, a new inhibitor or prolyl endopeptidase. //J.Antibiot. 1996. V.49(10). p. 1022−1025.
- Yee A.A., D.J.O'Neil. Uniform 15N labeling of fungal peptide: the structure and dynamics of an alamethicin by 15N and 'H NMR spectroscopy. //Biochem. 1992. V.31. p.3135−3143.
- Esposito G., Carver J., Boyd J., Campbell I. High-resolution 'H-NMR study of the solution structure of alamethicin. //Biochemistry, 1987, Y.26, p. 1043−1050.
- Sansom P. Alamethicin and related peptaibols model ion channels //Eur Biophys. J., 1993, V.22, P.105−124.
- You S., Peng S., LienL., Breed J., Sansom P. Engineering stabilized ion channels: Covalent dimers of alamethicin. //Biochemistry, 1996, V.35, p.6225−6232.
- Molle G., Duclohier H., Julien S., Spach G. Synthetic analogues of alamethicin: effect of C-terminal residue substitutionand chain length on the ion channel lifetimes. //Biochim. Biophys. Acta, 1991, V. 1064(2), p.365−369.
- Molle Q., Davoust D., Brachais L. Influence of the conformation of alamethicin on channel lifetimes.//Int. J. Pept. Protein Res., 1995, V.47, P.159−164.
- Kaduk C., Duclohier H., Dathe M., et. al. Influence of proline position upon the ion channel activity of alamethicin. //Biophys. J., 1997, V.72, P.2151−2159.
- Kaduk C., Dathe M., Bienert M. Functional modifications of alamethicin ion channels by substitution of glutamine 7, glicine 11 and proline 14. //Biochim. Biophys. Acta, 1998, V.1373(l), P. 137−146.
- Isabella L., Karle I., Iudith L., et al. Crystal structure of Leu-Zervamicin, a membrane ion channel peptide.// Proc. Nat. Acad. Sci. USA, 1991, V.88, P.5307−53 011.
- Sanson M.S.P., Balaram P., Karle I. Ion channel formation by zervamicin IIB. //Eur. Biophys.J., 1993, V.21, P.369−383.
- Nilges M., Brunger A. Automated modeling of coiled coils: application to the GCN4 dimerization region. //Prot. Engineer., 1997, V.4, P.649−659.
- Karle I., Agarwalla S., Balaram P. Agating mechanism of channels formed by zervamicins. //Biopolymers, 1994, V.34, P.721−735.
- Chul M.-C.et al. MR-387A and B, new aminopeptidase N inhibitors. //J.Antibiot. 1996. V.49(l). P.99−102.
- Hook D.J. et al. Integrated byological-physicochemocal system for the identification of antitumor compounds in fermentation broths. //J.Cromatogr. 1987. V.385(l) p.99−108.
- Burkhardt K., Fiedler H.-P. New cineromicins and musacins obtained by metabolite pattern analysis of Streptomices griseoviridis (FH-S 1832). //J.Antibiot. 1996. V.49(5). P.432−437.
- Marinelli F. et al. Antibiotic GE37468A a new inhibitor of bacterial protein synthesis. //J.Antibiot. 1996. V.49(9). P.880−885.
- Егоров H.C., Олескин A.B. Биотехнология: проблемы и перспективы. //М.:Высшая школа, 1987.
- Bierbaum G. et al. Cloning, sequensing and production of the lantabiotic mersacidin. //FEMS Microbiol. Lett. 1995. 15- 127(1−2). P.121−126.
- Arroyo-Flores B.L. et al. Biosyntesis of glicoproteins in Candida albcans. //PMID:9 850 415, UI:99 067 401
- Kang Y. et al. Characterisation of genes involved in byosinthesis of as novel antibiotic from Burkholderia cepacia ВС 11 and their role in biological control of Rhosoctonoa solani. //Appl.Env.Microbiol. 1998.64(10). P.3939−3947.
- Bu’Lock J.D. Industrial aspects of biochemistry. // North Holland Publ., 1974, V. l, pp.293−342.
- Vining L.C. Secondary metabolism. //Biotecnology, 1986, Y.4, pp. 20−38.
- O’Sullivan J., Ball C. Biochemistry and genetic regulation of commercially important antibiotics. // Addison-Wesley Publ., Massachusets, 1985, pp. 1 -15
- Omura S. Trends in the search for bioactive microbial metabolites. //J. of Industrial Microbiology, 1992, V.10, pp.135−156.
- Borchert S., Patil S.S., Marahiel M.A. Identification of putative multifunctional peptide synthetase genes using highly conserved oligonucleotide sequences derived from known synthetases. //FEMS Microbiol.Lett., 1992,71(2), 175−80.
- Marahiel M.A., Nakano M.M., Zuber P. Regulation of peptide antibiotic production in Bacillus. //Mol.Microbiol., 1993,7(5), 631−36.
- Fuma S., Fujishima Y., Corbell N. Nucleotide sequence of 5' portion of srfA that contains the region required for competence establishment in Bacillus subtilus. //Nucleic Acids Res., 1993,21(1), 93−97
- Kleinkauf H. Nonribosomal biosynthesis of peptide antibiotics. //Eur.J.Biochem., 1990, V.192(l), p.1−15.
- Stachelhaus Т., Marahiel M.A. Modular structure of genes encoding multifunctional peptide synthetases required for non-ribosomal peptide synthesis. //FEMS Microbiol.Lett., 1995,125(1), 3−14
- Schwartz D., Alijah R. The peptide synthetase gene phsA from Streptomyces viridochromogenes is not juxtaposed with other genes involved in nonribosomal biosynthesis of peptides. //Appl.Environ.Microbiol., 1996,62(2), 570−77.
- Пшеничникова А.Б., Карнаухова Е. Н., Звонкова Е. Н., Швец В. И. Методы получения дейтерированных аминокислот. /Обзорная статья/. //Биорганическая химия, 1995, т.21, No.3, с. 163−178.
- Griffiths, D. V., Feeney, J., Roberts, G. С. K., and Burgen, A. S. V. Preparation of selectively deuterated aromatic amino acids for use in 'H NMR studies of proteins. //Biochim. et Biophys. Acta, 1976, V. 446, p. 479−485.
- Мосин О. В, Складнее Д. А., Егорова Т. А., Швец В. И. Методы получения0 1Я 1аминокислот и белков, меченных стабильными изотопами ZH, 1JC, N, 100. //Биотехнология, 1996, т.22, No. 10, с.24−40.
- Egorova-Zachernuk Т.A., Shvets V.I. et al. Preparation of site-specific isotopically labelled zervamicins. //J.Pept.Sci. 1996. V.2(6). P.341−350.
- Liu K., White L.R. et al. Biosyntesis of armetomicin. //J.Antibiot. 1995. V.48(4). P.347−348.
- O’Hagan D., Rogers S.V. The biosynthesis of monensin-A. //J.Antibiot. 1995. V.48(ll). P.1280−1287.
- Kuo M.S. et al. Biosynthesis of macrofortine-A. //J.Antibiot. 1996. V.49(10). P.1006−1013.
- Staley A.S., Rinehart K.L. Biosyntesis of the streptovaricins. //J.Antibiot. 1991. V.44(2). P.218−224.
- Trani A. et al. Deaminoteicoplanin and its derivatives. //J.Med.Chem. 1989. V.32(2). P.310−314.
- Herrin T.R. et al. Preparation of biologically active ristocetin derivatives: replacements of the Г-amino group. //J.Med.Chem. 28(9). 1371−1375.
- Римави В. Химический синтез изотопно-меченого зервамицина IIB. /Диссертация на соискание ученой степени кандидата наук/. //Москва, 2000.
- Akaji К., Tamai Y., Kiso Y. Efficient synthesis of peptaibol using a chloroimidazolidium coupling reagent. //Tefrahedron, 1997, V.53, P.567−584.
- Slomczynska U., Zarbrocki J., Kaczmarek K. Facilitated synthesis of peptaibpls: alamethicin via enzymatic segment condensation. //Biopolymers, 1992, V.32(l 1), P.1461−1470.
- Ogrel A., Bloemhoff W., Lugtenburg J., Raap J. Total synthesis of zervamicin IIB and its deuterium-labelled analogues. //J. Pept. Sci., 1997, V.3(3), P. 193−208.
- Ogrel A., Bloemhoff W., Lugtenburg J., Raap J. Synthesis of the isotibically labelled C-terminal fragment of zervamicin IIB: Approach to the synthesis of Aib-containing peptides. //Liebigs Ann. Chem., 1997, V.12, p.41−47.
- Ogrel A., Ogrel S., Shvets V., Raap J. Synthesis of the 15N-Gln labelled peptaibol antibiotic zervamicin IIB. //Letters in Peptide Science, 1998, V.5 (2−3), P.175−178.
- Хеншен A. M. ВЭЖХ в биохимии. //Мир, 1988.
- Kajimura Y, Kaneda M. Fusaricidin A, a new depsipeptide antibiotic produced by Bac. polymyxa KT-8. //J.Antibiot. 1996. V.49(2) P.129−135.
- Argoudelis A.D., Dietz A., Johnson L.E., Zervamicins I and II, polypeptide antibiotics produced by Emericellopsis salmosynnemata. //J. Antibiotics. 1974. Vol. 27(5), p. 321 -328.
- Argoudelis A.D., Dietz A., Johnson L.E. Antibiotics Zervamicins I and II and process for preparing the same. //C.A 84:15685k, Patent USA, № 3.907.990, 1975.
- Krishna K., Balaram P. Structural chemestry and membrane modifying activity of fungal polypeptides zervamicins, antiamoebins and efrapeptins. //Appl.Chem., 1990,62(7), 1417−20.
- Hermodson M., Mahoney W.C. Separation of Peptides by Reversed-Phase HPLC. //Methodsi n enzymology. 1983. Vol. 91, p.352 359.
- Mant C.T. Optimization of peptide separation in HPLC. //J.Chromatography. 1989. Vol. 12, p. l39- 172.
- Рогожкииа E.A., Еремин C.B., Швец В. И., Складнев Д. А. Биотехнологическое получение стабильносеменных препаратов зервамицина IIB. //Хим.-Фарм. Журнал.-2000.-т.34.-№ 6.-с.37−40.
- Kumazawa. S. et all. Structual elucidation of aibellin. //J.of Antibiotics. 1994. Vol. 47(10), p. l 136−1144.
- Ogrel A.A. Total synthesis of specifically stable isotope labeled zervamicin IIB, an antibiotic peptaibol produced by Emericellopsis salmosynnemata. //Proefschrift ter verijging van de graad van Doctor Leiden. 1965.
- Flaumenhaft E., Bose S., Crespi H.L. Deuterium isotope effects in cytology. /Int.Rev/. //Cytol. 1965. Vol.18, p. 313−361.
- Рогожкина E.A., Еремин C.B., Швец В.И.,. Складнев Д. А. Метод экспресс-анализа зервамицина ИВ в биомассе E.salmosynnemata. //Хим.-Фарм. Журнал.-2000.-т.34.-№ 6.-с.50−53.
- Leclerc G. et al. Directed biosynthesis of peptaibol antibiotics in two Trichoderma strains. //J.Antibiot. 1998. Vol. 51(2).- p.170−177.
- Рогожкина E.A., Пономарёва E.B., Швец В. И., Овчинникова Т. В., Складнев Д. А., Раап Я. Получение препарата пептидного антибиотика зервамицина, тотально-меченого стабильными изотопами углерода и азота.// Биотехнология. 2001, в печати.
- Nona D.A., Blake M.I., Crespi H.L. Effects of deuterium oxide on the culturing of Penicillum janczewskii //J.Pharm.Sci. 1968. V.57, No.6, p.975−979.
- Crespi H.L., Marmur J., Katz J.J. Use of fully deuterated algae extracts for the isolation of nucleic acids. // Contribution from the Argonne National Laboratory and the Graduate Department of Biochemistry, Brandes university, 1962.
- Crespi H.L. The isolation of deuterated bacteriorhodopsin from fully deuterated Halohacterium halobium. //Methods in Enzymology. 1982 V.88, p. 1−12.
- Мосин О. В, Складнев Д. А., Юркевич А. М., Швец В. И. Исследование процесса адаптации бактерий к тяжелой воде. // Биотехнология. 1996 № 9, с.105−109.
- Мосин О. В, Складнев Д. А., Швец В. И. Изучение биосинтеза аминокислот штаммов Brevibacterium methylicum при росте на средах, содержащих тяжелую воду и дейтерометанол. //Биотехнология. 1996 № 3, с.3−12.
- Мосин О. В, Казаринова JI. А., Преображенская Е. С., Складнев Д. А., Рост бактерии Bacillus subtilis и биосинтез инозина на высокодейтерированной среде. // Биотехнология, 1996, № 4, с.85−94.
- Крылов И.А., Красноштанова А. А., Манаков М. Н. Кислотный гидролиз белковых веществ биомассы промышленных микроорганизмов. 3. Кинетика кислотной экстракции белковых веществ из клеток дрожжей и бактерий. //Биотехнология, 1996, No.3, с.50−55.
- Березин И.В., Рабинович М. Л., Синицын А. П. Исследование возможностей кинетического метода определения глюкозы. //Биохимия, 1977, т.24, No9, с. 16 311 636.