Serendipitous discovery of an unexpected rearrangement leads to two new classes of potential protease inhibitors.
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.
Zhong
Jiaying
J
Department of Chemistry, Wichita State University, Wichita, KS 67260, USA.
Lai
Zhong
Z
Groutas
Christopher S
CS
Wong
Tzutshin
T
Gan
Xiangdong
X
Alliston
Kevin R
KR
Eichhorn
David
D
Hoidal
John R
JR
Groutas
William C
WC
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
D015842:Serine Proteinase Inhibitors; D013449:Sulfonamides; D012697:Serine Endopeptidases; D019272:Leukocyte Elastase; D053146:Myeloblastin