Synthesis and structure-activity relationships of elafin, an elastase-specific inhibitor
Elafin, an elastase-specific inhibitor isolated from human skin, and its related peptides were synthesized by the solution procedure, and their inhibitory activities were measured against various enzymes. During the oxidative folding reactions of the reduced peptides, the ratio of the active product...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1992-06, Vol.185 (3), p.967-973 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Tsunemi, Masahiko Kato, Hisao Nishiuchi, Yuji Kumagaye, Shin-ichiro Sakakibara, Shumpei |
| description | Elafin, an elastase-specific inhibitor isolated from human skin, and its related peptides were synthesized by the solution procedure, and their inhibitory activities were measured against various enzymes. During the oxidative folding reactions of the reduced peptides, the ratio of the active product to the inactive product was varied by changing the concentration of guanidine HCl and the amount of redox reagents. The disulfide structures of fully active synthetic elafin and the inactive product were determined by amino acid analysis, gas-phase sequencing and mass spectrometry of their proteolytic fragments. The relationship between structure and inhibitory activities and/or the folding reaction was examined and the amino terminal part of the elafin molecule was found to have a great influence on the folding reactions, but not on the inhibitory activities. |
| doi_str_mv | 10.1016/0006-291X(92)91721-2 |
| format | Article |
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Psychology</topic><topic>Humans</topic><topic>Hydrolases</topic><topic>Indicators and Reagents</topic><topic>Kinetics</topic><topic>Molecular Sequence Data</topic><topic>Pancreatic Elastase - antagonists & inhibitors</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - pharmacology</topic><topic>Protein Conformation</topic><topic>Proteinase Inhibitory Proteins, Secretory</topic><topic>Proteins</topic><topic>Serine Proteinase Inhibitors - chemical synthesis</topic><topic>Serine Proteinase Inhibitors - pharmacology</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tsunemi, Masahiko</creatorcontrib><creatorcontrib>Kato, Hisao</creatorcontrib><creatorcontrib>Nishiuchi, Yuji</creatorcontrib><creatorcontrib>Kumagaye, Shin-ichiro</creatorcontrib><creatorcontrib>Sakakibara, Shumpei</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>Tsunemi, Masahiko</au><au>Kato, Hisao</au><au>Nishiuchi, Yuji</au><au>Kumagaye, Shin-ichiro</au><au>Sakakibara, Shumpei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Synthesis and structure-activity relationships of elafin, an elastase-specific inhibitor</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1992-06-30</date><risdate>1992</risdate><volume>185</volume><issue>3</issue><spage>967</spage><epage>973</epage><pages>967-973</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>Elafin, an elastase-specific inhibitor isolated from human skin, and its related peptides were synthesized by the solution procedure, and their inhibitory activities were measured against various enzymes. During the oxidative folding reactions of the reduced peptides, the ratio of the active product to the inactive product was varied by changing the concentration of guanidine HCl and the amount of redox reagents. The disulfide structures of fully active synthetic elafin and the inactive product were determined by amino acid analysis, gas-phase sequencing and mass spectrometry of their proteolytic fragments. The relationship between structure and inhibitory activities and/or the folding reaction was examined and the amino terminal part of the elafin molecule was found to have a great influence on the folding reactions, but not on the inhibitory activities.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>1627147</pmid><doi>10.1016/0006-291X(92)91721-2</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1992-06, Vol.185 (3), p.967-973 |
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| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cattle Disulfides - analysis Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Humans Hydrolases Indicators and Reagents Kinetics Molecular Sequence Data Pancreatic Elastase - antagonists & inhibitors Peptides - chemical synthesis Peptides - pharmacology Protein Conformation Proteinase Inhibitory Proteins, Secretory Proteins Serine Proteinase Inhibitors - chemical synthesis Serine Proteinase Inhibitors - pharmacology Structure-Activity Relationship |
| title | Synthesis and structure-activity relationships of elafin, an elastase-specific inhibitor |
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