{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,10,8]],"date-time":"2023-10-08T10:12:26Z","timestamp":1696759946366},"reference-count":26,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2011,5,13]],"date-time":"2011-05-13T00:00:00Z","timestamp":1305244800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Peptide Science"],"published-print":{"date-parts":[[2011,8]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>HTLV\u2010I is a debilitating and\/or lethal retrovirus that causes HTLV\u2010I\u2010associated myelopathy\/tropical spastic paraparesis, adult T\u2010cell leukemia and several inflammatory diseases. HTLV\u2010I protease is an aspartic retropepsin involved in HTLV\u2010I replication and its inhibition could treatHTLV\u2010I infection. A recombinant L40I mutant HTLV\u2010I protease was designed and obtained from <jats:italic>Escherichia coli<\/jats:italic>, self\u2010processingand purification by ion\u2010exchange chromatography. The protease was refolded by a one\u2010step dialysis and recovered activity. The cleavage efficiency of the [Ile<jats:sup>40<\/jats:sup>]HTLV\u2010I protease was at least 300 times higher for a fluorescent substratethan that of our previously reported recombinant His\u2010tagged non\u2010mutated HTLV\u2010I protease. In addition, we designed and synthesized a substrate containing a highly fluorescent Mca moiety in the fragment before the scissile bond, and a chromogenic <jats:italic>p<\/jats:italic>\u2010nitrophenylalanine moiety after the scissile bond that greatly amplified spectrometry detection and improved the HTLV\u2010I protease inhibition potency assay. The HTLV\u2010I protease inhibition assay with the [Ile<jats:sup>40<\/jats:sup>]HTLV\u2010I protease and fluorogenic substrate requires distinctively less protease, substrate, inhibitor and assay time than our previous methods. This means our new assay is more cost\u2010effective and more time\u2010efficient while being reproducible and less labor\u2010intensive. Copyright \u00a9 2011 European Peptide Society and John Wiley &amp; Sons, Ltd.<\/jats:p>","DOI":"10.1002\/psc.1375","type":"journal-article","created":{"date-parts":[[2011,5,13]],"date-time":"2011-05-13T14:17:39Z","timestamp":1305296259000},"page":"569-575","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Development of [Ile<sup>40<\/sup>]HTLV\u2010I protease inhibition assay using novel fluorogenic and chromogenic 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