Evaluation of peptide-aldehyde inhibitors using R188I mutant of SARS 3CL protease as a proteolysis-resistant mutant
Identifieur interne : 000284 ( PascalFrancis/Checkpoint ); précédent : 000283; suivant : 000285Evaluation of peptide-aldehyde inhibitors using R188I mutant of SARS 3CL protease as a proteolysis-resistant mutant
Auteurs : Kenichi Akaji [Japon] ; Hiroyuki Konno [Japon] ; Mari Onozuka [Japon] ; Ayumi Makino [Japon] ; Hiroyuki Saito [Japon] ; Kazuto Nosaka [Japon]Source :
- Bioorganic & medicinal chemistry [ 0968-0896 ] ; 2008.
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Abstract
The 3C-like (3CL) protease of the severe acute respiratory syndrome (SARS) coronavirus is a key enzyme for the virus maturation. We found for the first time that the mature SARS 3CL protease is subject to degradation at 188Arg/189Gln. Replacing Arg with lle at position 188 rendered the protease resistant to proteolysis. The R188I mutant digested a conserved undecapeptide substrate with a Km of 33.8 μM and kcat of 4753 s-1. Compared with the value reported for the mature protease containing a C-terminal His-tag, the relative activity of the mutant was nearly 106. Novel peptide-aldehyde derivatives containing a side-chain-protected C-terminal Gln efficiently inhibited the catalytic activity of the R188I mutant. The results indicated for the first time that the tetrapeptide sequence is enough for inhibitory activities of peptide-aldehyde derivatives.
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Medicine</s1><s2>Kita-ku, Kyoto 603-8334</s2><s3>JPN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Japon</country><wicri:noRegion>Kita-ku, Kyoto 603-8334</wicri:noRegion></affiliation></author><author><name sortKey="Onozuka, Mari" sort="Onozuka, Mari" uniqKey="Onozuka M" first="Mari" last="Onozuka">Mari Onozuka</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Department of Chemistry, Graduate School of Medical Science, Kyoto Prefectural University of Medicine</s1><s2>Kita-ku, Kyoto 603-8334</s2><s3>JPN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Japon</country><wicri:noRegion>Kita-ku, Kyoto 603-8334</wicri:noRegion></affiliation></author><author><name sortKey="Makino, Ayumi" sort="Makino, Ayumi" uniqKey="Makino A" first="Ayumi" last="Makino">Ayumi Makino</name><affiliation wicri:level="1"><inist:fA14 i1="02"><s1>Department of Biophysical Chemistry, Kobe Pharmaceutical University</s1><s2>Kobe 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wicri:level="1"><inist:fA14 i1="01"><s1>Department of Chemistry, Graduate School of Medical Science, Kyoto Prefectural University of Medicine</s1><s2>Kita-ku, Kyoto 603-8334</s2><s3>JPN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Japon</country><wicri:noRegion>Kita-ku, Kyoto 603-8334</wicri:noRegion></affiliation></author><author><name sortKey="Konno, Hiroyuki" sort="Konno, Hiroyuki" uniqKey="Konno H" first="Hiroyuki" last="Konno">Hiroyuki Konno</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Department of Chemistry, Graduate School of Medical Science, Kyoto Prefectural University of Medicine</s1><s2>Kita-ku, Kyoto 603-8334</s2><s3>JPN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Japon</country><wicri:noRegion>Kita-ku, Kyoto 603-8334</wicri:noRegion></affiliation></author><author><name sortKey="Onozuka, Mari" sort="Onozuka, Mari" uniqKey="Onozuka M" first="Mari" last="Onozuka">Mari Onozuka</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Department of Chemistry, Graduate School of Medical Science, Kyoto Prefectural University of Medicine</s1><s2>Kita-ku, Kyoto 603-8334</s2><s3>JPN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Japon</country><wicri:noRegion>Kita-ku, Kyoto 603-8334</wicri:noRegion></affiliation></author><author><name sortKey="Makino, Ayumi" sort="Makino, Ayumi" uniqKey="Makino A" first="Ayumi" last="Makino">Ayumi Makino</name><affiliation wicri:level="1"><inist:fA14 i1="02"><s1>Department of Biophysical Chemistry, Kobe Pharmaceutical University</s1><s2>Kobe 658-8558</s2><s3>JPN</s3><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Japon</country><wicri:noRegion>Kobe 658-8558</wicri:noRegion></affiliation></author><author><name sortKey="Saito, Hiroyuki" sort="Saito, Hiroyuki" uniqKey="Saito H" first="Hiroyuki" last="Saito">Hiroyuki Saito</name><affiliation wicri:level="1"><inist:fA14 i1="02"><s1>Department of Biophysical Chemistry, Kobe Pharmaceutical University</s1><s2>Kobe 658-8558</s2><s3>JPN</s3><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Japon</country><wicri:noRegion>Kobe 658-8558</wicri:noRegion></affiliation></author><author><name sortKey="Nosaka, Kazuto" sort="Nosaka, Kazuto" uniqKey="Nosaka K" first="Kazuto" last="Nosaka">Kazuto Nosaka</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Department of Chemistry, Graduate School of Medical Science, Kyoto Prefectural University of Medicine</s1><s2>Kita-ku, Kyoto 603-8334</s2><s3>JPN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Japon</country><wicri:noRegion>Kita-ku, Kyoto 603-8334</wicri:noRegion></affiliation></author></analytic><series><title level="j" type="main">Bioorganic & medicinal chemistry</title><title level="j" type="abbreviated">Bioorg. med. chem.</title><idno type="ISSN">0968-0896</idno><imprint><date when="2008">2008</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Bioorganic & medicinal chemistry</title><title level="j" type="abbreviated">Bioorg. med. chem.</title><idno type="ISSN">0968-0896</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aldehyde</term><term>Biological activity</term><term>Chemical synthesis</term><term>Cysteine endopeptidases</term><term>Enzyme inhibitor</term><term>Hydrolysis resistance</term><term>In vitro</term><term>Mutation</term><term>Peptide synthesis</term><term>Peptides</term><term>Protease inhibitor</term><term>Severe acute respiratory syndrome virus</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Peptide</term><term>Aldéhyde</term><term>Inhibiteur protease</term><term>Mutation</term><term>Cysteine endopeptidases</term><term>Virus syndrome respiratoire aigu sévère</term><term>Résistance hydrolyse</term><term>Activité biologique</term><term>Synthèse chimique</term><term>Synthèse peptidique</term><term>In vitro</term><term>Inhibiteur enzyme</term><term>Glutamique acide(acétylthréonyl-séryl-alanyl-valyl-leucyl-1-désoxy)</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The 3C-like (3CL) protease of the severe acute respiratory syndrome (SARS) coronavirus is a key enzyme for the virus maturation. We found for the first time that the mature SARS 3CL protease is subject to degradation at 188Arg/189Gln. Replacing Arg with lle at position 188 rendered the protease resistant to proteolysis. The R188I mutant digested a conserved undecapeptide substrate with a K<sub>m</sub> of 33.8 μM and k<sub>cat</sub> of 4753 s<sup>-1</sup>. Compared with the value reported for the mature protease containing a C-terminal His-tag, the relative activity of the mutant was nearly 10<sup>6</sup>. Novel peptide-aldehyde derivatives containing a side-chain-protected C-terminal Gln efficiently inhibited the catalytic activity of the R188I mutant. The results indicated for the first time that the tetrapeptide sequence is enough for inhibitory activities of peptide-aldehyde derivatives.</div></front></TEI><inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>0968-0896</s0></fA01><fA03 i2="1"><s0>Bioorg. med. chem.</s0></fA03><fA05><s2>16</s2></fA05><fA06><s2>21</s2></fA06><fA08 i1="01" i2="1" l="ENG"><s1>Evaluation of peptide-aldehyde inhibitors using R188I mutant of SARS 3CL protease as a proteolysis-resistant mutant</s1></fA08><fA11 i1="01" i2="1"><s1>AKAJI (Kenichi)</s1></fA11><fA11 i1="02" i2="1"><s1>KONNO (Hiroyuki)</s1></fA11><fA11 i1="03" i2="1"><s1>ONOZUKA (Mari)</s1></fA11><fA11 i1="04" i2="1"><s1>MAKINO (Ayumi)</s1></fA11><fA11 i1="05" i2="1"><s1>SAITO (Hiroyuki)</s1></fA11><fA11 i1="06" i2="1"><s1>NOSAKA (Kazuto)</s1></fA11><fA14 i1="01"><s1>Department of Chemistry, Graduate School of Medical Science, Kyoto Prefectural University of Medicine</s1><s2>Kita-ku, Kyoto 603-8334</s2><s3>JPN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>6 aut.</sZ></fA14><fA14 i1="02"><s1>Department of Biophysical Chemistry, Kobe Pharmaceutical University</s1><s2>Kobe 658-8558</s2><s3>JPN</s3><sZ>4 aut.</sZ><sZ>5 aut.</sZ></fA14><fA20><s1>9400-9408</s1></fA20><fA21><s1>2008</s1></fA21><fA23 i1="01"><s0>ENG</s0></fA23><fA43 i1="01"><s1>INIST</s1><s2>26564</s2><s5>354000185936900010</s5></fA43><fA44><s0>0000</s0><s1>© 2009 INIST-CNRS. All rights reserved.</s1></fA44><fA47 i1="01" i2="1"><s0>09-0041831</s0></fA47><fA60><s1>P</s1></fA60><fA61><s0>A</s0></fA61><fA64 i1="01" i2="1"><s0>Bioorganic & medicinal chemistry</s0></fA64><fA66 i1="01"><s0>GBR</s0></fA66><fA99><s0>1/2 p.ref. et notes</s0></fA99><fC01 i1="01" l="ENG"><s0>The 3C-like (3CL) protease of the severe acute respiratory syndrome (SARS) coronavirus is a key enzyme for the virus maturation. We found for the first time that the mature SARS 3CL protease is subject to degradation at 188Arg/189Gln. Replacing Arg with lle at position 188 rendered the protease resistant to proteolysis. The R188I mutant digested a conserved undecapeptide substrate with a K<sub>m</sub> of 33.8 μM and k<sub>cat</sub> of 4753 s<sup>-1</sup>. Compared with the value reported for the mature protease containing a C-terminal His-tag, the relative activity of the mutant was nearly 10<sup>6</sup>. Novel peptide-aldehyde derivatives containing a side-chain-protected C-terminal Gln efficiently inhibited the catalytic activity of the R188I mutant. The results indicated for the first time that the tetrapeptide sequence is enough for inhibitory activities of peptide-aldehyde derivatives.</s0></fC01><fC02 i1="01" i2="X"><s0>002B02S05</s0></fC02><fC03 i1="01" i2="X" l="FRE"><s0>Peptide</s0><s5>01</s5></fC03><fC03 i1="01" i2="X" l="ENG"><s0>Peptides</s0><s5>01</s5></fC03><fC03 i1="01" i2="X" l="SPA"><s0>Péptido</s0><s5>01</s5></fC03><fC03 i1="02" i2="X" l="FRE"><s0>Aldéhyde</s0><s5>02</s5></fC03><fC03 i1="02" i2="X" l="ENG"><s0>Aldehyde</s0><s5>02</s5></fC03><fC03 i1="02" i2="X" l="SPA"><s0>Aldehído</s0><s5>02</s5></fC03><fC03 i1="03" i2="X" l="FRE"><s0>Inhibiteur protease</s0><s2>FR</s2><s5>03</s5></fC03><fC03 i1="03" i2="X" l="ENG"><s0>Protease inhibitor</s0><s2>FR</s2><s5>03</s5></fC03><fC03 i1="03" i2="X" l="SPA"><s0>Inhibidor proteasa</s0><s2>FR</s2><s5>03</s5></fC03><fC03 i1="04" i2="X" l="FRE"><s0>Mutation</s0><s5>04</s5></fC03><fC03 i1="04" i2="X" l="ENG"><s0>Mutation</s0><s5>04</s5></fC03><fC03 i1="04" i2="X" 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acide(acétylthréonyl-séryl-alanyl-valyl-leucyl-1-désoxy)</s0><s4>INC</s4><s5>76</s5></fC03><fC07 i1="01" i2="X" l="FRE"><s0>Peptidases</s0><s2>FE</s2></fC07><fC07 i1="01" i2="X" l="ENG"><s0>Peptidases</s0><s2>FE</s2></fC07><fC07 i1="01" i2="X" l="SPA"><s0>Peptidases</s0><s2>FE</s2></fC07><fC07 i1="02" i2="X" l="FRE"><s0>Hydrolases</s0><s2>FE</s2></fC07><fC07 i1="02" i2="X" l="ENG"><s0>Hydrolases</s0><s2>FE</s2></fC07><fC07 i1="02" i2="X" l="SPA"><s0>Hydrolases</s0><s2>FE</s2></fC07><fC07 i1="03" i2="X" l="FRE"><s0>Enzyme</s0><s2>FE</s2></fC07><fC07 i1="03" i2="X" l="ENG"><s0>Enzyme</s0><s2>FE</s2></fC07><fC07 i1="03" i2="X" l="SPA"><s0>Enzima</s0><s2>FE</s2></fC07><fC07 i1="04" i2="X" l="FRE"><s0>Coronavirus</s0><s2>NW</s2></fC07><fC07 i1="04" i2="X" l="ENG"><s0>Coronavirus</s0><s2>NW</s2></fC07><fC07 i1="04" i2="X" l="SPA"><s0>Coronavirus</s0><s2>NW</s2></fC07><fC07 i1="05" i2="X" l="FRE"><s0>Coronaviridae</s0><s2>NW</s2></fC07><fC07 i1="05" i2="X" l="ENG"><s0>Coronaviridae</s0><s2>NW</s2></fC07><fC07 i1="05" i2="X" l="SPA"><s0>Coronaviridae</s0><s2>NW</s2></fC07><fC07 i1="06" i2="X" l="FRE"><s0>Nidovirales</s0><s2>NW</s2></fC07><fC07 i1="06" i2="X" l="ENG"><s0>Nidovirales</s0><s2>NW</s2></fC07><fC07 i1="06" i2="X" l="SPA"><s0>Nidovirales</s0><s2>NW</s2></fC07><fC07 i1="07" i2="X" l="FRE"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="07" i2="X" l="ENG"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="07" i2="X" l="SPA"><s0>Virus</s0><s2>NW</s2></fC07><fN21><s1>026</s1></fN21></pA></standard></inist><affiliations><list><country><li>Japon</li></country></list><tree><country name="Japon"><noRegion><name sortKey="Akaji, Kenichi" sort="Akaji, Kenichi" uniqKey="Akaji K" first="Kenichi" last="Akaji">Kenichi Akaji</name></noRegion><name sortKey="Konno, Hiroyuki" sort="Konno, Hiroyuki" uniqKey="Konno H" first="Hiroyuki" last="Konno">Hiroyuki Konno</name><name sortKey="Makino, Ayumi" sort="Makino, Ayumi" uniqKey="Makino A" first="Ayumi" last="Makino">Ayumi Makino</name><name sortKey="Nosaka, Kazuto" sort="Nosaka, Kazuto" uniqKey="Nosaka K" first="Kazuto" last="Nosaka">Kazuto Nosaka</name><name sortKey="Onozuka, Mari" sort="Onozuka, Mari" uniqKey="Onozuka M" first="Mari" last="Onozuka">Mari Onozuka</name><name sortKey="Saito, Hiroyuki" sort="Saito, Hiroyuki" uniqKey="Saito H" first="Hiroyuki" last="Saito">Hiroyuki Saito</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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