Significant effects of Z-Gln-Val-Val-OMe, common sequences of thiol proteinase inhibitors on thiol proteinases
The first studies on a series of the small synthetic thiol proteinase inhibitors, conservative common sequences in several thiol proteinase inhibitors, are described. Among the many interesting findings with synthetic thiol proteinase inhibitors was the observation that the most effective analogue,...
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Veröffentlicht in: | Biochemical and biophysical research communications 1987-03, Vol.143 (2), p.749-752 |
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description | The first studies on a series of the small synthetic thiol proteinase inhibitors, conservative common sequences in several thiol proteinase inhibitors, are described. Among the many interesting findings with synthetic thiol proteinase inhibitors was the observation that the most effective analogue, Z-Gln-Val-Val-Ala-Gly-OMe, whose amino and carboxyl groups were protected with Z and OMe, respectively, showed inhibitory activity on papain and cathepsin B and protected papain from egg cystatin, human low-molecular-weight kininogen and T-kininogen-induced inhibition but not from leupeptin-induced inhibition. Moreover, it was revealed that Z-Gln-Val-Val-OMe was the smallest peptide to exhibit a protective effect on papain. |
doi_str_mv | 10.1016/0006-291X(87)91417-3 |
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Among the many interesting findings with synthetic thiol proteinase inhibitors was the observation that the most effective analogue, Z-Gln-Val-Val-Ala-Gly-OMe, whose amino and carboxyl groups were protected with Z and OMe, respectively, showed inhibitory activity on papain and cathepsin B and protected papain from egg cystatin, human low-molecular-weight kininogen and T-kininogen-induced inhibition but not from leupeptin-induced inhibition. Moreover, it was revealed that Z-Gln-Val-Val-OMe was the smallest peptide to exhibit a protective effect on papain.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Applied sciences</subject><subject>Binding Sites</subject><subject>Binding, Competitive</subject><subject>Cathepsin B - antagonists & inhibitors</subject><subject>Cystatins</subject><subject>Exact sciences and technology</subject><subject>Kininogens - antagonists & inhibitors</subject><subject>Kininogens - pharmacology</subject><subject>Leupeptins - antagonists & inhibitors</subject><subject>Oligopeptides - chemical synthesis</subject><subject>Oligopeptides - metabolism</subject><subject>Oligopeptides - pharmacology</subject><subject>Other techniques and industries</subject><subject>Papain - antagonists & inhibitors</subject><subject>Protease Inhibitors</subject><subject>Proteins - pharmacology</subject><subject>Structure-Activity Relationship</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU1LHTEUhoNU7NX6D1qYRZEWnPZkMklmNoJIawsWF1YRNyHJnNSUmUSTuYX-e3M_uJtCFyGL9zkn5zwh5C2FTxSo-AwAom56ev-hkx972lJZsz2yoNBD3VBoX5HFDnlNDnP-DUBpK_oDcsC4ELIVCxJu_K_gnbc6zBU6h3bOVXTVQ305hvpOj-tz_QNPKxunKYYq4_MSg8U1Nj_6OFZPKc7og85Y-fDojZ9jKnH4J85vyL7TY8bj7X1Ebr9--Xnxrb66vvx-cX5VW9aJue4EsMZY0cnBdhwHwZzpOq4HidbSBlhvLDfOGK5R9LZ3hnEjsWwLFKzs2RE52fQtb5dx86wmny2Oow4Yl1lJ2UrgTVPAdgPaFHNO6NRT8pNOfxUFtdKsVg7VyqHqpFprVqyUvdv2X5oJh13R1mvJ329zna0eXdLB-rzDJGfAqSzY2QbD4uKPx6Sy9Su5g0_lJ9QQ_f_neAH5TJp8</recordid><startdate>19870313</startdate><enddate>19870313</enddate><creator>Teno, N.</creator><creator>Tsuboi, S.</creator><creator>Itoh, N.</creator><creator>Okamoto, H.</creator><creator>Okada, Y.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19870313</creationdate><title>Significant effects of Z-Gln-Val-Val-OMe, common sequences of thiol proteinase inhibitors on thiol proteinases</title><author>Teno, N. ; Tsuboi, S. ; Itoh, N. ; Okamoto, H. ; Okada, Y.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-86032bc687dc85ed63fb885ad7ecc12039bc5bfbb5ae69c9fb35b7e006010c793</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Applied sciences</topic><topic>Binding Sites</topic><topic>Binding, Competitive</topic><topic>Cathepsin B - antagonists & inhibitors</topic><topic>Cystatins</topic><topic>Exact sciences and technology</topic><topic>Kininogens - antagonists & inhibitors</topic><topic>Kininogens - pharmacology</topic><topic>Leupeptins - antagonists & inhibitors</topic><topic>Oligopeptides - chemical synthesis</topic><topic>Oligopeptides - metabolism</topic><topic>Oligopeptides - pharmacology</topic><topic>Other techniques and industries</topic><topic>Papain - antagonists & inhibitors</topic><topic>Protease Inhibitors</topic><topic>Proteins - pharmacology</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Teno, N.</creatorcontrib><creatorcontrib>Tsuboi, S.</creatorcontrib><creatorcontrib>Itoh, N.</creatorcontrib><creatorcontrib>Okamoto, H.</creatorcontrib><creatorcontrib>Okada, Y.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Teno, N.</au><au>Tsuboi, S.</au><au>Itoh, N.</au><au>Okamoto, H.</au><au>Okada, Y.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Significant effects of Z-Gln-Val-Val-OMe, common sequences of thiol proteinase inhibitors on thiol proteinases</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1987-03-13</date><risdate>1987</risdate><volume>143</volume><issue>2</issue><spage>749</spage><epage>752</epage><pages>749-752</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>The first studies on a series of the small synthetic thiol proteinase inhibitors, conservative common sequences in several thiol proteinase inhibitors, are described. Among the many interesting findings with synthetic thiol proteinase inhibitors was the observation that the most effective analogue, Z-Gln-Val-Val-Ala-Gly-OMe, whose amino and carboxyl groups were protected with Z and OMe, respectively, showed inhibitory activity on papain and cathepsin B and protected papain from egg cystatin, human low-molecular-weight kininogen and T-kininogen-induced inhibition but not from leupeptin-induced inhibition. Moreover, it was revealed that Z-Gln-Val-Val-OMe was the smallest peptide to exhibit a protective effect on papain.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>3566746</pmid><doi>10.1016/0006-291X(87)91417-3</doi><tpages>4</tpages></addata></record> |
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subjects | Amino Acid Sequence Animals Applied sciences Binding Sites Binding, Competitive Cathepsin B - antagonists & inhibitors Cystatins Exact sciences and technology Kininogens - antagonists & inhibitors Kininogens - pharmacology Leupeptins - antagonists & inhibitors Oligopeptides - chemical synthesis Oligopeptides - metabolism Oligopeptides - pharmacology Other techniques and industries Papain - antagonists & inhibitors Protease Inhibitors Proteins - pharmacology Structure-Activity Relationship |
title | Significant effects of Z-Gln-Val-Val-OMe, common sequences of thiol proteinase inhibitors on thiol proteinases |
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