Stability of N-Derivatized and .alpha.-Methyl Analogs of Aspartame to Hydrolysis by Mammalian Cell-Surface Peptidases
The biological stability of the N-derivatized (N-formyl, N-formylcarbamoyl, and N-carbamoyl) and alpha-methyl analogues of aspartame (L-alpha-aspartyl-L-phenylalanine methyl ester; APM) to hydrolysis by human and porcine intestinal and kidney microvillar membranes and by purified preparations of the...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 1994-07, Vol.42 (7), p.1397-1401 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Hooper, Nigel M. Hesp, Richard J. Tieku, Stephen Boesten, Willy H. J. Toniolo, Claudio Kamphuis, Johan |
| description | The biological stability of the N-derivatized (N-formyl, N-formylcarbamoyl, and N-carbamoyl) and alpha-methyl analogues of aspartame (L-alpha-aspartyl-L-phenylalanine methyl ester; APM) to hydrolysis by human and porcine intestinal and kidney microvillar membranes and by purified preparations of the cell-surface peptidases aminopeptidase A (EC 3.4.11.7) and aminopeptidase W (EC 3.4.11.16) has been examined. Of the N-derivatized analogues of APM, only N-formylcarbamoyl-APM was hydrolyzed slightly by the human and porcine intestinal microvillar membrane preparations [1.1 mmol min(-1) (mg of protein)(-1) as compared to 80.1 nmol min(-1) (mg of protein)(-1) for APM with the human jejunal microvillar membranes]. However, the pattern of inhibition of the hydrolysis of N-formylcarbamoyl-APM was distinct from that observed for APM, being inhibited ( 80%) by actinonin or 1,10-phenanthroline but not by amastatin, bestatin, or rentiapril. In contrast to APM, N-formylcarbamoyl-APM and the other N-derivatized analogues of APM were resistant to hydrolysis by aminopeptidases A and W. All of the alpha-methyl derivatives of APM were resistant to hydrolysis by both the microvillar membrane preparations and the purified peptidases |
| doi_str_mv | 10.1021/jf00043a001 |
| format | Article |
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J. ; Toniolo, Claudio ; Kamphuis, Johan</creator><creatorcontrib>Hooper, Nigel M. ; Hesp, Richard J. ; Tieku, Stephen ; Boesten, Willy H. J. ; Toniolo, Claudio ; Kamphuis, Johan</creatorcontrib><description>The biological stability of the N-derivatized (N-formyl, N-formylcarbamoyl, and N-carbamoyl) and alpha-methyl analogues of aspartame (L-alpha-aspartyl-L-phenylalanine methyl ester; APM) to hydrolysis by human and porcine intestinal and kidney microvillar membranes and by purified preparations of the cell-surface peptidases aminopeptidase A (EC 3.4.11.7) and aminopeptidase W (EC 3.4.11.16) has been examined. Of the N-derivatized analogues of APM, only N-formylcarbamoyl-APM was hydrolyzed slightly by the human and porcine intestinal microvillar membrane preparations [1.1 mmol min(-1) (mg of protein)(-1) as compared to 80.1 nmol min(-1) (mg of protein)(-1) for APM with the human jejunal microvillar membranes]. However, the pattern of inhibition of the hydrolysis of N-formylcarbamoyl-APM was distinct from that observed for APM, being inhibited ( 80%) by actinonin or 1,10-phenanthroline but not by amastatin, bestatin, or rentiapril. In contrast to APM, N-formylcarbamoyl-APM and the other N-derivatized analogues of APM were resistant to hydrolysis by aminopeptidases A and W. All of the alpha-methyl derivatives of APM were resistant to hydrolysis by both the microvillar membrane preparations and the purified peptidases</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf00043a001</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>ASPARTAME ; ASPARTAMO ; Biological and medical sciences ; CERDO ; Food additives ; Food industries ; Fundamental and applied biological sciences. Psychology ; General aspects ; GENERO HUMANO ; GENRE HUMAIN ; HIDROLISIS ; HYDROLYSE ; INTESTIN ; INTESTINOS ; MEMBRANA MUCOSA ; MEMBRANAS CELULARES ; MEMBRANE CELLULAIRE ; MUQUEUSE ; PEPTIDASAS ; PEPTIDASE ; PORCIN ; REIN ; RINONES</subject><ispartof>Journal of agricultural and food chemistry, 1994-07, Vol.42 (7), p.1397-1401</ispartof><rights>1995 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a281t-6d609d776897cca66d52384227a175cb746ab19911f3ccb75b38a48f4e71b0cf3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jf00043a001$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf00043a001$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>315,781,785,2766,27078,27926,27927,56740,56790</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3420791$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Hooper, Nigel M.</creatorcontrib><creatorcontrib>Hesp, Richard J.</creatorcontrib><creatorcontrib>Tieku, Stephen</creatorcontrib><creatorcontrib>Boesten, Willy H. J.</creatorcontrib><creatorcontrib>Toniolo, Claudio</creatorcontrib><creatorcontrib>Kamphuis, Johan</creatorcontrib><title>Stability of N-Derivatized and .alpha.-Methyl Analogs of Aspartame to Hydrolysis by Mammalian Cell-Surface Peptidases</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>The biological stability of the N-derivatized (N-formyl, N-formylcarbamoyl, and N-carbamoyl) and alpha-methyl analogues of aspartame (L-alpha-aspartyl-L-phenylalanine methyl ester; APM) to hydrolysis by human and porcine intestinal and kidney microvillar membranes and by purified preparations of the cell-surface peptidases aminopeptidase A (EC 3.4.11.7) and aminopeptidase W (EC 3.4.11.16) has been examined. Of the N-derivatized analogues of APM, only N-formylcarbamoyl-APM was hydrolyzed slightly by the human and porcine intestinal microvillar membrane preparations [1.1 mmol min(-1) (mg of protein)(-1) as compared to 80.1 nmol min(-1) (mg of protein)(-1) for APM with the human jejunal microvillar membranes]. However, the pattern of inhibition of the hydrolysis of N-formylcarbamoyl-APM was distinct from that observed for APM, being inhibited ( 80%) by actinonin or 1,10-phenanthroline but not by amastatin, bestatin, or rentiapril. In contrast to APM, N-formylcarbamoyl-APM and the other N-derivatized analogues of APM were resistant to hydrolysis by aminopeptidases A and W. All of the alpha-methyl derivatives of APM were resistant to hydrolysis by both the microvillar membrane preparations and the purified peptidases</description><subject>ASPARTAME</subject><subject>ASPARTAMO</subject><subject>Biological and medical sciences</subject><subject>CERDO</subject><subject>Food additives</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects</subject><subject>GENERO HUMANO</subject><subject>GENRE HUMAIN</subject><subject>HIDROLISIS</subject><subject>HYDROLYSE</subject><subject>INTESTIN</subject><subject>INTESTINOS</subject><subject>MEMBRANA MUCOSA</subject><subject>MEMBRANAS CELULARES</subject><subject>MEMBRANE CELLULAIRE</subject><subject>MUQUEUSE</subject><subject>PEPTIDASAS</subject><subject>PEPTIDASE</subject><subject>PORCIN</subject><subject>REIN</subject><subject>RINONES</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><recordid>eNptkE1r3DAQhkVpoNukp9560qHQQ9FWsi1LPi6bNClsPsDJpRcxlqVEW-3aSNpS59dHi0vooadheJ4ZZl6EPjK6ZLRg37aWUlqVQCl7gxaMF5RwxuRbtKAZE8lr9g69j3GbNckFXaBDm6Bz3qUJDxbfkHMT3G9I7tn0GPY9XoIfn2BJrk16mjxe7cEPj_HoruIIIcHO4DTgq6kPg5-ii7ib8DXsduAd7PHaeE_aQ7CgDb4zY3I9RBPP0IkFH82Hv_UUPXy_uF9fkc3t5Y_1akOgkCyRuq9p0wtRy0ZoDXXd86KUVVEIYILrTlQ1dKxpGLOlzi3vSgmVtJURrKPalqfo67xXhyHGYKwag9tBmBSj6piY-iexbH-e7RGiBm8D7LWLryNlVVDRHDUyay4m8-cVQ_ilalEKru7vWnUufzZVe7lRRfY_zb6FQcFjyCsf2oYznh_L8MsMQUe1HQ4hBxz_e90LNASOjA</recordid><startdate>19940701</startdate><enddate>19940701</enddate><creator>Hooper, Nigel M.</creator><creator>Hesp, Richard J.</creator><creator>Tieku, Stephen</creator><creator>Boesten, Willy H. J.</creator><creator>Toniolo, Claudio</creator><creator>Kamphuis, Johan</creator><general>American Chemical Society</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>19940701</creationdate><title>Stability of N-Derivatized and .alpha.-Methyl Analogs of Aspartame to Hydrolysis by Mammalian Cell-Surface Peptidases</title><author>Hooper, Nigel M. ; Hesp, Richard J. ; Tieku, Stephen ; Boesten, Willy H. J. ; Toniolo, Claudio ; Kamphuis, Johan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a281t-6d609d776897cca66d52384227a175cb746ab19911f3ccb75b38a48f4e71b0cf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>ASPARTAME</topic><topic>ASPARTAMO</topic><topic>Biological and medical sciences</topic><topic>CERDO</topic><topic>Food additives</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects</topic><topic>GENERO HUMANO</topic><topic>GENRE HUMAIN</topic><topic>HIDROLISIS</topic><topic>HYDROLYSE</topic><topic>INTESTIN</topic><topic>INTESTINOS</topic><topic>MEMBRANA MUCOSA</topic><topic>MEMBRANAS CELULARES</topic><topic>MEMBRANE CELLULAIRE</topic><topic>MUQUEUSE</topic><topic>PEPTIDASAS</topic><topic>PEPTIDASE</topic><topic>PORCIN</topic><topic>REIN</topic><topic>RINONES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hooper, Nigel M.</creatorcontrib><creatorcontrib>Hesp, Richard J.</creatorcontrib><creatorcontrib>Tieku, Stephen</creatorcontrib><creatorcontrib>Boesten, Willy H. J.</creatorcontrib><creatorcontrib>Toniolo, Claudio</creatorcontrib><creatorcontrib>Kamphuis, Johan</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hooper, Nigel M.</au><au>Hesp, Richard J.</au><au>Tieku, Stephen</au><au>Boesten, Willy H. J.</au><au>Toniolo, Claudio</au><au>Kamphuis, Johan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Stability of N-Derivatized and .alpha.-Methyl Analogs of Aspartame to Hydrolysis by Mammalian Cell-Surface Peptidases</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>1994-07-01</date><risdate>1994</risdate><volume>42</volume><issue>7</issue><spage>1397</spage><epage>1401</epage><pages>1397-1401</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>The biological stability of the N-derivatized (N-formyl, N-formylcarbamoyl, and N-carbamoyl) and alpha-methyl analogues of aspartame (L-alpha-aspartyl-L-phenylalanine methyl ester; APM) to hydrolysis by human and porcine intestinal and kidney microvillar membranes and by purified preparations of the cell-surface peptidases aminopeptidase A (EC 3.4.11.7) and aminopeptidase W (EC 3.4.11.16) has been examined. Of the N-derivatized analogues of APM, only N-formylcarbamoyl-APM was hydrolyzed slightly by the human and porcine intestinal microvillar membrane preparations [1.1 mmol min(-1) (mg of protein)(-1) as compared to 80.1 nmol min(-1) (mg of protein)(-1) for APM with the human jejunal microvillar membranes]. However, the pattern of inhibition of the hydrolysis of N-formylcarbamoyl-APM was distinct from that observed for APM, being inhibited ( 80%) by actinonin or 1,10-phenanthroline but not by amastatin, bestatin, or rentiapril. In contrast to APM, N-formylcarbamoyl-APM and the other N-derivatized analogues of APM were resistant to hydrolysis by aminopeptidases A and W. All of the alpha-methyl derivatives of APM were resistant to hydrolysis by both the microvillar membrane preparations and the purified peptidases</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><doi>10.1021/jf00043a001</doi><tpages>5</tpages></addata></record> |
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| ispartof | Journal of agricultural and food chemistry, 1994-07, Vol.42 (7), p.1397-1401 |
| issn | 0021-8561 1520-5118 |
| language | eng |
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| source | American Chemical Society Journals |
| subjects | ASPARTAME ASPARTAMO Biological and medical sciences CERDO Food additives Food industries Fundamental and applied biological sciences. Psychology General aspects GENERO HUMANO GENRE HUMAIN HIDROLISIS HYDROLYSE INTESTIN INTESTINOS MEMBRANA MUCOSA MEMBRANAS CELULARES MEMBRANE CELLULAIRE MUQUEUSE PEPTIDASAS PEPTIDASE PORCIN REIN RINONES |
| title | Stability of N-Derivatized and .alpha.-Methyl Analogs of Aspartame to Hydrolysis by Mammalian Cell-Surface Peptidases |
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