Novel inhibitors of human leukocyte elastase and cathepsin G. Sequence variants of squash seed protease inhibitor with altered protease selectivity
Novel peptide inhibitors of human leukocyte elastase (HLE) and cathepsin G (CG) were prepared by solid-phase peptide synthesis of P1 amino acid sequence variants of Curcurbita maxima trypsin inhibitor III (CMTI-III), a 29-residue peptide found in squash seed. A systematic study of P1 variants indica...
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| Veröffentlicht in: | Biochemistry (Easton) 1989-07, Vol.28 (14), p.5708-5714 |
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| container_issue | 14 |
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| creator | McWherter, Charles A Walkenhorst, William F Campbell, Edward J Glover, George I |
| description | Novel peptide inhibitors of human leukocyte elastase (HLE) and cathepsin G (CG) were prepared by solid-phase peptide synthesis of P1 amino acid sequence variants of Curcurbita maxima trypsin inhibitor III (CMTI-III), a 29-residue peptide found in squash seed. A systematic study of P1 variants indicated that P1 Arg, Lys, Leu, Ala, Phe, and Met inhibit trypsin; P1 Val, Ile, Gly, Leu, Ala, Phe, and Met inhibit HLE; P1 Leu, Ala, Phe, and Met inhibit CG and chymotrypsin. Variants with P1 Val, Ile, or Gly were selective inhibitors of HLE, while inhibition of trypsin required P1 amino acids with an unbranched beta carbon. Studies of Val-5-CMTI-III (P1 Val) inhibition of HLE demonstrated a 1:1 binding stoichiometry with a (K sub(i)) sub(app) of 8.7 nM. Inhibition of HLE by Gly-5-CMTI-III indicated a significant role for reactive-site structural moieties other than the P1 side chain. |
| doi_str_mv | 10.1021/bi00440a002 |
| format | Article |
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Sequence variants of squash seed protease inhibitor with altered protease selectivity</title><source>MEDLINE</source><source>ACS Journals</source><creator>McWherter, Charles A ; Walkenhorst, William F ; Campbell, Edward J ; Glover, George I</creator><creatorcontrib>McWherter, Charles A ; Walkenhorst, William F ; Campbell, Edward J ; Glover, George I</creatorcontrib><description>Novel peptide inhibitors of human leukocyte elastase (HLE) and cathepsin G (CG) were prepared by solid-phase peptide synthesis of P1 amino acid sequence variants of Curcurbita maxima trypsin inhibitor III (CMTI-III), a 29-residue peptide found in squash seed. A systematic study of P1 variants indicated that P1 Arg, Lys, Leu, Ala, Phe, and Met inhibit trypsin; P1 Val, Ile, Gly, Leu, Ala, Phe, and Met inhibit HLE; P1 Leu, Ala, Phe, and Met inhibit CG and chymotrypsin. Variants with P1 Val, Ile, or Gly were selective inhibitors of HLE, while inhibition of trypsin required P1 amino acids with an unbranched beta carbon. Studies of Val-5-CMTI-III (P1 Val) inhibition of HLE demonstrated a 1:1 binding stoichiometry with a (K sub(i)) sub(app) of 8.7 nM. Inhibition of HLE by Gly-5-CMTI-III indicated a significant role for reactive-site structural moieties other than the P1 side chain.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00440a002</identifier><identifier>PMID: 2775732</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>550201 - Biochemistry- Tracer Techniques ; AMINO ACID SEQUENCE ; Analytical, structural and metabolic biochemistry ; ANIMALS ; BASIC BIOLOGICAL SCIENCES ; BETA DECAY RADIOISOTOPES ; Binding Sites ; BIOCHEMISTRY ; Biological and medical sciences ; BIOLOGICAL MATERIALS ; BLOOD ; BLOOD CELLS ; BLOOD COAGULATION FACTORS ; BODY FLUIDS ; catalytic activity ; Cathepsin G ; CATHEPSINS ; Cathepsins - antagonists & inhibitors ; CHEMICAL REACTIONS ; CHEMISTRY ; COAGULANTS ; Cucurbita maxima ; Curcubita maxima ; DAYS LIVING RADIOISOTOPES ; DECOMPOSITION ; DRUGS ; elastase ; ELECTRON CAPTURE RADIOISOTOPES ; ENZYMATIC HYDROLYSIS ; ENZYME INHIBITORS ; ENZYMES ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Genetic Variation ; HEMATOLOGIC AGENTS ; Humans ; HYDROLASES ; HYDROLYSIS ; In Vitro Techniques ; INFLAMMATION ; INTERMEDIATE MASS NUCLEI ; IODINE 125 ; IODINE ISOTOPES ; ISOTOPES ; Kinetics ; LEUKOCYTES ; Leukocytes - enzymology ; LYSIS ; MAMMALS ; MAN ; MATERIALS ; MOLECULAR STRUCTURE ; NUCLEI ; ODD-EVEN NUCLEI ; ORGANIC COMPOUNDS ; Pancreatic Elastase - antagonists & inhibitors ; Pancreatic Elastase - blood ; PATHOLOGICAL CHANGES ; PEPTIDE HYDROLASES ; PRIMATES ; Protease Inhibitors - genetics ; Protease Inhibitors - pharmacology ; proteinase inhibitors ; PROTEINS ; RADIOISOTOPES ; seeds ; Seeds - analysis ; Serine Endopeptidases ; SERINE PROTEINASES ; SH-PROTEINASES ; SOLVOLYSIS ; SYMPTOMS ; TRYPSIN ; VERTEBRATES</subject><ispartof>Biochemistry (Easton), 1989-07, Vol.28 (14), p.5708-5714</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a466t-e72913d6b29e99b308d3611811d22a4342526046238eb82bc376d47c86e9d9743</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/bi00440a002$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00440a002$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,780,784,885,2763,27074,27922,27923,56736,56786</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19298663$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2775732$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/5030607$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>McWherter, Charles A</creatorcontrib><creatorcontrib>Walkenhorst, William F</creatorcontrib><creatorcontrib>Campbell, Edward J</creatorcontrib><creatorcontrib>Glover, George I</creatorcontrib><title>Novel inhibitors of human leukocyte elastase and cathepsin G. Sequence variants of squash seed protease inhibitor with altered protease selectivity</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Novel peptide inhibitors of human leukocyte elastase (HLE) and cathepsin G (CG) were prepared by solid-phase peptide synthesis of P1 amino acid sequence variants of Curcurbita maxima trypsin inhibitor III (CMTI-III), a 29-residue peptide found in squash seed. A systematic study of P1 variants indicated that P1 Arg, Lys, Leu, Ala, Phe, and Met inhibit trypsin; P1 Val, Ile, Gly, Leu, Ala, Phe, and Met inhibit HLE; P1 Leu, Ala, Phe, and Met inhibit CG and chymotrypsin. Variants with P1 Val, Ile, or Gly were selective inhibitors of HLE, while inhibition of trypsin required P1 amino acids with an unbranched beta carbon. Studies of Val-5-CMTI-III (P1 Val) inhibition of HLE demonstrated a 1:1 binding stoichiometry with a (K sub(i)) sub(app) of 8.7 nM. Inhibition of HLE by Gly-5-CMTI-III indicated a significant role for reactive-site structural moieties other than the P1 side chain.</description><subject>550201 - Biochemistry- Tracer Techniques</subject><subject>AMINO ACID SEQUENCE</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>ANIMALS</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>BETA DECAY RADIOISOTOPES</subject><subject>Binding Sites</subject><subject>BIOCHEMISTRY</subject><subject>Biological and medical sciences</subject><subject>BIOLOGICAL MATERIALS</subject><subject>BLOOD</subject><subject>BLOOD CELLS</subject><subject>BLOOD COAGULATION FACTORS</subject><subject>BODY FLUIDS</subject><subject>catalytic activity</subject><subject>Cathepsin G</subject><subject>CATHEPSINS</subject><subject>Cathepsins - antagonists & inhibitors</subject><subject>CHEMICAL REACTIONS</subject><subject>CHEMISTRY</subject><subject>COAGULANTS</subject><subject>Cucurbita maxima</subject><subject>Curcubita maxima</subject><subject>DAYS LIVING RADIOISOTOPES</subject><subject>DECOMPOSITION</subject><subject>DRUGS</subject><subject>elastase</subject><subject>ELECTRON CAPTURE RADIOISOTOPES</subject><subject>ENZYMATIC HYDROLYSIS</subject><subject>ENZYME INHIBITORS</subject><subject>ENZYMES</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic Variation</subject><subject>HEMATOLOGIC AGENTS</subject><subject>Humans</subject><subject>HYDROLASES</subject><subject>HYDROLYSIS</subject><subject>In Vitro Techniques</subject><subject>INFLAMMATION</subject><subject>INTERMEDIATE MASS NUCLEI</subject><subject>IODINE 125</subject><subject>IODINE ISOTOPES</subject><subject>ISOTOPES</subject><subject>Kinetics</subject><subject>LEUKOCYTES</subject><subject>Leukocytes - enzymology</subject><subject>LYSIS</subject><subject>MAMMALS</subject><subject>MAN</subject><subject>MATERIALS</subject><subject>MOLECULAR STRUCTURE</subject><subject>NUCLEI</subject><subject>ODD-EVEN NUCLEI</subject><subject>ORGANIC COMPOUNDS</subject><subject>Pancreatic Elastase - antagonists & inhibitors</subject><subject>Pancreatic Elastase - blood</subject><subject>PATHOLOGICAL CHANGES</subject><subject>PEPTIDE HYDROLASES</subject><subject>PRIMATES</subject><subject>Protease Inhibitors - genetics</subject><subject>Protease Inhibitors - pharmacology</subject><subject>proteinase inhibitors</subject><subject>PROTEINS</subject><subject>RADIOISOTOPES</subject><subject>seeds</subject><subject>Seeds - analysis</subject><subject>Serine Endopeptidases</subject><subject>SERINE PROTEINASES</subject><subject>SH-PROTEINASES</subject><subject>SOLVOLYSIS</subject><subject>SYMPTOMS</subject><subject>TRYPSIN</subject><subject>VERTEBRATES</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV9rFDEUxQex1LX65LMYCtoHmZp_k0wepdhWWLSwLT6GTOauk3Z2sk0yq_s5_MKmzrL2QfAhhHB-9-RcTlG8IviUYEo-NA5jzrHBmD4pZqSiuORKVU-LGcZYlFQJ_Kx4HuNtfnIs-WFxSKWsJKOz4tcXv4EeuaFzjUs-ROSXqBtXZkA9jHfebhMg6E1MJgIyQ4usSR2soxvQxSlawP0IgwW0McGZIf0Zj_ejiR2KAC1aB5_gYXT_A_rhUodMnyA81iP0YJPbuLR9URwsTR_h5e4-Km7OP12fXZbzrxefzz7OS8OFSCVIqghrRUMVKNUwXLdMEFIT0lJqOOO0ogJzQVkNTU0by6RoubS1ANUqydlRcTz5-picjtYlsJ31w5CD6AozLLDM0LsJyknzrjHplYsW-t4M4MeopSIqn_-DpGJCSUwy-H4CbfAxBljqdXArE7aaYP1QqH5UaKZf72zHZgXtnt01mPW3O91Ea_plMIN18a-loqoWgmWunDgXE_zc6ybcaSGZrPT11UJXl-RbNb-q9Hnm30z80nhtvofsebOgOT6mQhIucCZOJsLYqG_9GIZc1j93-A3q2c04</recordid><startdate>19890711</startdate><enddate>19890711</enddate><creator>McWherter, Charles A</creator><creator>Walkenhorst, William F</creator><creator>Campbell, Edward J</creator><creator>Glover, George I</creator><general>American Chemical Society</general><scope>FBQ</scope><scope>BSCLL</scope><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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>19890711</creationdate><title>Novel inhibitors of human leukocyte elastase and cathepsin G. Sequence variants of squash seed protease inhibitor with altered protease selectivity</title><author>McWherter, Charles A ; Walkenhorst, William F ; Campbell, Edward J ; Glover, George I</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a466t-e72913d6b29e99b308d3611811d22a4342526046238eb82bc376d47c86e9d9743</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>550201 - Biochemistry- Tracer Techniques</topic><topic>AMINO ACID SEQUENCE</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>ANIMALS</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>BETA DECAY RADIOISOTOPES</topic><topic>Binding Sites</topic><topic>BIOCHEMISTRY</topic><topic>Biological and medical sciences</topic><topic>BIOLOGICAL MATERIALS</topic><topic>BLOOD</topic><topic>BLOOD CELLS</topic><topic>BLOOD COAGULATION FACTORS</topic><topic>BODY FLUIDS</topic><topic>catalytic activity</topic><topic>Cathepsin G</topic><topic>CATHEPSINS</topic><topic>Cathepsins - antagonists & inhibitors</topic><topic>CHEMICAL REACTIONS</topic><topic>CHEMISTRY</topic><topic>COAGULANTS</topic><topic>Cucurbita maxima</topic><topic>Curcubita maxima</topic><topic>DAYS LIVING RADIOISOTOPES</topic><topic>DECOMPOSITION</topic><topic>DRUGS</topic><topic>elastase</topic><topic>ELECTRON CAPTURE RADIOISOTOPES</topic><topic>ENZYMATIC HYDROLYSIS</topic><topic>ENZYME INHIBITORS</topic><topic>ENZYMES</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetic Variation</topic><topic>HEMATOLOGIC AGENTS</topic><topic>Humans</topic><topic>HYDROLASES</topic><topic>HYDROLYSIS</topic><topic>In Vitro Techniques</topic><topic>INFLAMMATION</topic><topic>INTERMEDIATE MASS NUCLEI</topic><topic>IODINE 125</topic><topic>IODINE ISOTOPES</topic><topic>ISOTOPES</topic><topic>Kinetics</topic><topic>LEUKOCYTES</topic><topic>Leukocytes - enzymology</topic><topic>LYSIS</topic><topic>MAMMALS</topic><topic>MAN</topic><topic>MATERIALS</topic><topic>MOLECULAR STRUCTURE</topic><topic>NUCLEI</topic><topic>ODD-EVEN NUCLEI</topic><topic>ORGANIC COMPOUNDS</topic><topic>Pancreatic Elastase - antagonists & inhibitors</topic><topic>Pancreatic Elastase - blood</topic><topic>PATHOLOGICAL CHANGES</topic><topic>PEPTIDE HYDROLASES</topic><topic>PRIMATES</topic><topic>Protease Inhibitors - genetics</topic><topic>Protease Inhibitors - pharmacology</topic><topic>proteinase inhibitors</topic><topic>PROTEINS</topic><topic>RADIOISOTOPES</topic><topic>seeds</topic><topic>Seeds - analysis</topic><topic>Serine Endopeptidases</topic><topic>SERINE PROTEINASES</topic><topic>SH-PROTEINASES</topic><topic>SOLVOLYSIS</topic><topic>SYMPTOMS</topic><topic>TRYPSIN</topic><topic>VERTEBRATES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McWherter, Charles A</creatorcontrib><creatorcontrib>Walkenhorst, William F</creatorcontrib><creatorcontrib>Campbell, Edward J</creatorcontrib><creatorcontrib>Glover, George I</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>McWherter, Charles A</au><au>Walkenhorst, William F</au><au>Campbell, Edward J</au><au>Glover, George I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Novel inhibitors of human leukocyte elastase and cathepsin G. Sequence variants of squash seed protease inhibitor with altered protease selectivity</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1989-07-11</date><risdate>1989</risdate><volume>28</volume><issue>14</issue><spage>5708</spage><epage>5714</epage><pages>5708-5714</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Novel peptide inhibitors of human leukocyte elastase (HLE) and cathepsin G (CG) were prepared by solid-phase peptide synthesis of P1 amino acid sequence variants of Curcurbita maxima trypsin inhibitor III (CMTI-III), a 29-residue peptide found in squash seed. A systematic study of P1 variants indicated that P1 Arg, Lys, Leu, Ala, Phe, and Met inhibit trypsin; P1 Val, Ile, Gly, Leu, Ala, Phe, and Met inhibit HLE; P1 Leu, Ala, Phe, and Met inhibit CG and chymotrypsin. Variants with P1 Val, Ile, or Gly were selective inhibitors of HLE, while inhibition of trypsin required P1 amino acids with an unbranched beta carbon. Studies of Val-5-CMTI-III (P1 Val) inhibition of HLE demonstrated a 1:1 binding stoichiometry with a (K sub(i)) sub(app) of 8.7 nM. Inhibition of HLE by Gly-5-CMTI-III indicated a significant role for reactive-site structural moieties other than the P1 side chain.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>2775732</pmid><doi>10.1021/bi00440a002</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-2960 |
| ispartof | Biochemistry (Easton), 1989-07, Vol.28 (14), p.5708-5714 |
| issn | 0006-2960 1520-4995 |
| language | eng |
| recordid | cdi_osti_scitechconnect_5030607 |
| source | MEDLINE; ACS Journals |
| subjects | 550201 - Biochemistry- Tracer Techniques AMINO ACID SEQUENCE Analytical, structural and metabolic biochemistry ANIMALS BASIC BIOLOGICAL SCIENCES BETA DECAY RADIOISOTOPES Binding Sites BIOCHEMISTRY Biological and medical sciences BIOLOGICAL MATERIALS BLOOD BLOOD CELLS BLOOD COAGULATION FACTORS BODY FLUIDS catalytic activity Cathepsin G CATHEPSINS Cathepsins - antagonists & inhibitors CHEMICAL REACTIONS CHEMISTRY COAGULANTS Cucurbita maxima Curcubita maxima DAYS LIVING RADIOISOTOPES DECOMPOSITION DRUGS elastase ELECTRON CAPTURE RADIOISOTOPES ENZYMATIC HYDROLYSIS ENZYME INHIBITORS ENZYMES Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Genetic Variation HEMATOLOGIC AGENTS Humans HYDROLASES HYDROLYSIS In Vitro Techniques INFLAMMATION INTERMEDIATE MASS NUCLEI IODINE 125 IODINE ISOTOPES ISOTOPES Kinetics LEUKOCYTES Leukocytes - enzymology LYSIS MAMMALS MAN MATERIALS MOLECULAR STRUCTURE NUCLEI ODD-EVEN NUCLEI ORGANIC COMPOUNDS Pancreatic Elastase - antagonists & inhibitors Pancreatic Elastase - blood PATHOLOGICAL CHANGES PEPTIDE HYDROLASES PRIMATES Protease Inhibitors - genetics Protease Inhibitors - pharmacology proteinase inhibitors PROTEINS RADIOISOTOPES seeds Seeds - analysis Serine Endopeptidases SERINE PROTEINASES SH-PROTEINASES SOLVOLYSIS SYMPTOMS TRYPSIN VERTEBRATES |
| title | Novel inhibitors of human leukocyte elastase and cathepsin G. Sequence variants of squash seed protease inhibitor with altered protease selectivity |
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