title: Serendipitous discovery of an unexpected rearrangement leads to two new classes of potential protease inhibitors.
abstract: The pathogenesis of a range of human diseases arises from the aberrant activity of proteolytic enzymes. Agents capable of selectively modulating the activity of these enzymes are of potential therapeutic value. Thus, there is a continuing need for the design of scaffolds that can be used in the development of new classes of protease inhibitors. We describe herein the serendipitous discovery of an unexpected rearrangement that leads to the formation of two novel templates that can be used in the design of protease inhibitors.
authors.affiliation: Department of Chemistry, Wichita State University, Wichita, KS 67260, USA.
authors.forename: Jiaying
authors.initials: J
authors.lastname: Zhong
authors.forename: Zhong
authors.initials: Z
authors.lastname: Lai
authors.forename: Christopher S
authors.initials: CS
authors.lastname: Groutas
authors.forename: Tzutshin
authors.initials: T
authors.lastname: Wong
authors.forename: Xiangdong
authors.initials: X
authors.lastname: Gan
authors.forename: Kevin R
authors.initials: KR
authors.lastname: Alliston
authors.forename: David
authors.initials: D
authors.lastname: Eichhorn
authors.forename: John R
authors.initials: JR
authors.lastname: Hoidal
authors.forename: William C
authors.initials: WC
authors.lastname: Groutas
mesh_terms: D006801:Humans; D007249:Inflammation / Q000188:drug therapy; D019272:Leukocyte Elastase / Q000037:antagonists & inhibitors; D015394:Molecular Structure; D053146:Myeloblastin; D012697:Serine Endopeptidases; D015842:Serine Proteinase Inhibitors / Q000138:chemical synthesis* / Q000494:pharmacology; D013329:Structure-Activity Relationship; D013449:Sulfonamides / Q000138:chemical synthesis / Q000494:pharmacology
chemical_list: D015842:Serine Proteinase Inhibitors; D013449:Sulfonamides; D012697:Serine Endopeptidases; D019272:Leukocyte Elastase; D053146:Myeloblastin