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pubmed-article:21392990pubmed:abstractTextThe human T cell leukemia/lymphotropic virus type 1 (HTLV-I) is clinically associated with adult T cell leukemia/lymphoma, HTLV-I associated myelopathy/tropical spastic paraparesis, and a number of other chronic inflammatory diseases. To stop the replication of the virus, we developed highly potent tetrapeptidic HTLV-I protease inhibitors. In a recent X-ray crystallography study, several of our inhibitors could not form co-crystal complexes with the protease due to their high hydrophobicity. In the current study, we designed, synthesized and evaluated the HTLV-I protease inhibition potency of compounds with hydrophilic end-capping moieties with the aim of improving pharmaceutic and pharmacokinetic properties.lld:pubmed
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pubmed-article:21392990pubmed:authorpubmed-author:KimuraTooruTlld:pubmed
pubmed-article:21392990pubmed:authorpubmed-author:KisoYoshiakiYlld:pubmed
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pubmed-article:21392990pubmed:authorpubmed-author:KumadaHenri-O...lld:pubmed
pubmed-article:21392990pubmed:copyrightInfoCopyright © 2011 Elsevier Ltd. All rights reserved.lld:pubmed
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pubmed-article:21392990pubmed:articleTitleDesign and synthesis of several small-size HTLV-I protease inhibitors with different hydrophilicity profiles.lld:pubmed
pubmed-article:21392990pubmed:affiliationDepartment of Medicinal Chemistry, Center for Frontier Research in Medicinal Science, Kyoto Pharmaceutical University, Yamashina-ku, Kyoto 607-8412, Japan.lld:pubmed
pubmed-article:21392990pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:21392990pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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