Synthesis and Study of Properties of Phosphinic Pseudo-Prolylglycylproline
Racemic phosphinic tripeptide 1 pyrrolidin-2-yl-{3-[(2-hydroxycarbonyl)-pyrrolidin-1-yl]-3-oxo-propyl}-phosphinic acid has been synthesized, its high resistance toward leucine aminopeptidase, carboxypeptidase Y, and the enzyme system of rat brain membranes has been shown. In vitro experiments with u...
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Veröffentlicht in: | Doklady. Chemistry 2021-05, Vol.498 (1), p.93-96 |
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creator | Shevchenko, K. V. Dmitriev, M. E. Vinyukov, A. V. Shevchenko, V. P. Kalashnikova, I. P. Nagaev, I. Yu Ragulin, V. V. Myasoedov, N. F. |
description | Racemic phosphinic tripeptide
1
pyrrolidin-2-yl-{3-[(2-hydroxycarbonyl)-pyrrolidin-1-yl]-3-oxo-propyl}-phosphinic acid has been synthesized, its high resistance toward leucine aminopeptidase, carboxypeptidase Y, and the enzyme system of rat brain membranes has been shown. In vitro experiments with using Semax synthetic peptide have shown that the effect of tripeptide
1
on the hydrolysis rate of Semax in the case of leucine aminopeptidase and carboxypeptidase Y is minimal. In experiments using the enzyme system of rat brain membranes, the decrease of the rate of Semax hydrolysis has been more evident. |
doi_str_mv | 10.1134/S001250082102004X |
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1
pyrrolidin-2-yl-{3-[(2-hydroxycarbonyl)-pyrrolidin-1-yl]-3-oxo-propyl}-phosphinic acid has been synthesized, its high resistance toward leucine aminopeptidase, carboxypeptidase Y, and the enzyme system of rat brain membranes has been shown. In vitro experiments with using Semax synthetic peptide have shown that the effect of tripeptide
1
on the hydrolysis rate of Semax in the case of leucine aminopeptidase and carboxypeptidase Y is minimal. In experiments using the enzyme system of rat brain membranes, the decrease of the rate of Semax hydrolysis has been more evident.</description><identifier>ISSN: 0012-5008</identifier><identifier>EISSN: 1608-3113</identifier><identifier>DOI: 10.1134/S001250082102004X</identifier><language>eng</language><publisher>Moscow: Pleiades Publishing</publisher><subject>Brain ; Chemistry ; Chemistry and Materials Science ; Chemistry/Food Science ; Enzymes ; High resistance ; Hydrolysis ; Industrial Chemistry/Chemical Engineering ; Leucine ; Membranes ; Rodents</subject><ispartof>Doklady. Chemistry, 2021-05, Vol.498 (1), p.93-96</ispartof><rights>Pleiades Publishing, Ltd. 2021. ISSN 0012-5008, Doklady Chemistry, 2021, Vol. 498, Part 1, pp. 93–96. © Pleiades Publishing, Ltd., 2021. Russian Text © The Author(s), 2021, published in Doklady Rossiiskoi Akademii Nauk. Khimiya, Nauki o Materialakh, 2021, Vol. 498, pp. 30–33.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c268t-548da338951dda3e76bb38b51de0860b4ebe402f9ba1fb5801615b4ce2a2865c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1134/S001250082102004X$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1134/S001250082102004X$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids></links><search><creatorcontrib>Shevchenko, K. V.</creatorcontrib><creatorcontrib>Dmitriev, M. E.</creatorcontrib><creatorcontrib>Vinyukov, A. V.</creatorcontrib><creatorcontrib>Shevchenko, V. P.</creatorcontrib><creatorcontrib>Kalashnikova, I. P.</creatorcontrib><creatorcontrib>Nagaev, I. Yu</creatorcontrib><creatorcontrib>Ragulin, V. V.</creatorcontrib><creatorcontrib>Myasoedov, N. F.</creatorcontrib><title>Synthesis and Study of Properties of Phosphinic Pseudo-Prolylglycylproline</title><title>Doklady. Chemistry</title><addtitle>Dokl Chem</addtitle><description>Racemic phosphinic tripeptide
1
pyrrolidin-2-yl-{3-[(2-hydroxycarbonyl)-pyrrolidin-1-yl]-3-oxo-propyl}-phosphinic acid has been synthesized, its high resistance toward leucine aminopeptidase, carboxypeptidase Y, and the enzyme system of rat brain membranes has been shown. In vitro experiments with using Semax synthetic peptide have shown that the effect of tripeptide
1
on the hydrolysis rate of Semax in the case of leucine aminopeptidase and carboxypeptidase Y is minimal. In experiments using the enzyme system of rat brain membranes, the decrease of the rate of Semax hydrolysis has been more evident.</description><subject>Brain</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chemistry/Food Science</subject><subject>Enzymes</subject><subject>High resistance</subject><subject>Hydrolysis</subject><subject>Industrial Chemistry/Chemical Engineering</subject><subject>Leucine</subject><subject>Membranes</subject><subject>Rodents</subject><issn>0012-5008</issn><issn>1608-3113</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNp1UEtLhUAUHqKg260f0E5obZ15Oi7j0pMLXbCgnTh6vHoxtRld-O8bM2gRrc53-F7wEXJJ4ZpSLm4SAMokgGYUGIB4PyIrqkCH3NPHZDXT4cyfkjPnDgAQR1yvyHMytUOFrnZB1hZBMozFFHRlsLNdj3ao0X1_Vef6qm7rPNg5HIsu9HwzNftmyqem97hu8ZyclFnj8OLnrsnb_d3r5jHcvjw8bW63Yc6UHkIpdJFxrmNJCw8wUsZwbfyHoBUYgQYFsDI2GS2N1EAVlUbkyDKmlcz5mlwtub73c0Q3pIdutK2vTJmMpIgh1sqr6KLKbeecxTLtbf2R2SmlkM6TpX8m8x62eJzXtnu0v8n_m74AZ6tt0g</recordid><startdate>20210501</startdate><enddate>20210501</enddate><creator>Shevchenko, K. V.</creator><creator>Dmitriev, M. E.</creator><creator>Vinyukov, A. V.</creator><creator>Shevchenko, V. P.</creator><creator>Kalashnikova, I. P.</creator><creator>Nagaev, I. Yu</creator><creator>Ragulin, V. V.</creator><creator>Myasoedov, N. F.</creator><general>Pleiades Publishing</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20210501</creationdate><title>Synthesis and Study of Properties of Phosphinic Pseudo-Prolylglycylproline</title><author>Shevchenko, K. V. ; Dmitriev, M. E. ; Vinyukov, A. V. ; Shevchenko, V. P. ; Kalashnikova, I. P. ; Nagaev, I. Yu ; Ragulin, V. V. ; Myasoedov, N. F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c268t-548da338951dda3e76bb38b51de0860b4ebe402f9ba1fb5801615b4ce2a2865c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Brain</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chemistry/Food Science</topic><topic>Enzymes</topic><topic>High resistance</topic><topic>Hydrolysis</topic><topic>Industrial Chemistry/Chemical Engineering</topic><topic>Leucine</topic><topic>Membranes</topic><topic>Rodents</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shevchenko, K. V.</creatorcontrib><creatorcontrib>Dmitriev, M. E.</creatorcontrib><creatorcontrib>Vinyukov, A. V.</creatorcontrib><creatorcontrib>Shevchenko, V. P.</creatorcontrib><creatorcontrib>Kalashnikova, I. P.</creatorcontrib><creatorcontrib>Nagaev, I. Yu</creatorcontrib><creatorcontrib>Ragulin, V. V.</creatorcontrib><creatorcontrib>Myasoedov, N. F.</creatorcontrib><collection>CrossRef</collection><jtitle>Doklady. Chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shevchenko, K. V.</au><au>Dmitriev, M. E.</au><au>Vinyukov, A. V.</au><au>Shevchenko, V. P.</au><au>Kalashnikova, I. P.</au><au>Nagaev, I. Yu</au><au>Ragulin, V. V.</au><au>Myasoedov, N. F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Synthesis and Study of Properties of Phosphinic Pseudo-Prolylglycylproline</atitle><jtitle>Doklady. Chemistry</jtitle><stitle>Dokl Chem</stitle><date>2021-05-01</date><risdate>2021</risdate><volume>498</volume><issue>1</issue><spage>93</spage><epage>96</epage><pages>93-96</pages><issn>0012-5008</issn><eissn>1608-3113</eissn><abstract>Racemic phosphinic tripeptide
1
pyrrolidin-2-yl-{3-[(2-hydroxycarbonyl)-pyrrolidin-1-yl]-3-oxo-propyl}-phosphinic acid has been synthesized, its high resistance toward leucine aminopeptidase, carboxypeptidase Y, and the enzyme system of rat brain membranes has been shown. In vitro experiments with using Semax synthetic peptide have shown that the effect of tripeptide
1
on the hydrolysis rate of Semax in the case of leucine aminopeptidase and carboxypeptidase Y is minimal. In experiments using the enzyme system of rat brain membranes, the decrease of the rate of Semax hydrolysis has been more evident.</abstract><cop>Moscow</cop><pub>Pleiades Publishing</pub><doi>10.1134/S001250082102004X</doi><tpages>4</tpages></addata></record> |
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subjects | Brain Chemistry Chemistry and Materials Science Chemistry/Food Science Enzymes High resistance Hydrolysis Industrial Chemistry/Chemical Engineering Leucine Membranes Rodents |
title | Synthesis and Study of Properties of Phosphinic Pseudo-Prolylglycylproline |
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