Please use this identifier to cite or link to this item:
Title: Biological evaluation and docking studies of natural isocoumarins as inhibitors for human kallikrein 5 and 7
Authors: Teixeira, Thiago S. P.
Freitas, Renato F.
Abrahao, Odonirio
Devienne, Karina F.
Souza, Lucas R. de
Blaber, Sachico I.
Blaber, Michael
Kondo, Marcia Y. [UNIFESP]
Juliano, Maria A. [UNIFESP]
Juliano, Luiz [UNIFESP]
Puzer, Luciano
Universidade Federal do ABC (UFABC)
Univ Fed Triangulo Mineiro
Florida State Univ
Universidade Federal de São Paulo (UNIFESP)
Keywords: Peptidases
Protease inhibitors
Issue Date: 15-Oct-2011
Publisher: Elsevier B.V.
Citation: Bioorganic & Medicinal Chemistry Letters. Oxford: Pergamon-Elsevier B.V., v. 21, n. 20, p. 6112-6115, 2011.
Abstract: Human kallikrein 5 and 7 (KLK5 and KLK7) are trypsin-like and chymotrypsin-like serine proteases, respectively, and promising targets for the treatment of skin desquamation, inflammation and cancer. in an effort to develop new inhibitors for these enzymes, we carried out enzymatic inhibition assays and docking studies with three isocoumarin compounds. Some promising inhibitors were uncovered, with vioxanthin and 8,8'-paepalantine being the most potent competitive inhibitors of KLK5 (K(i) = 22.9 mu M) and KLK7 (K(i) = 12.2 mu M), respectively. Our docking studies showed a good correlation with the experimental results, and revealed a distinct binding mode for the inhibitors at the binding sites of KLK5 and KLK7. in addition, the docking results suggested that the formation of hydrogen bonds at the oxyanion hole is essential for a good inhibitor. (C) 2011 Elsevier B.V. All rights reserved.
ISSN: 0960-894X
Other Identifiers:
Appears in Collections:Em verificação - Geral

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.