Please use this identifier to cite or link to this item:
|Title:||Amino derivatives of indole as potent inhibitors of isoprenylcysteine carboxyl methyltransferase||Authors:||Go, M.-L.
|Issue Date:||14-Oct-2010||Citation:||Go, M.-L., Leow, J.L., Gorla, S.K., Schüller, A.P., Wang, M., Casey, P.J. (2010-10-14). Amino derivatives of indole as potent inhibitors of isoprenylcysteine carboxyl methyltransferase. Journal of Medicinal Chemistry 53 (19) : 6838-6850. ScholarBank@NUS Repository. https://doi.org/10.1021/jm1002843||Abstract:||The enzyme isoprenylcysteine carboxyl methyltransferase (Icmt) plays an important role in the post-translational modification of proteins that are involved in the regulation of cell growth. The indole acetamide cysmethynil is by far the most potent and widely investigated Icmt inhibitor, but it has modest antiproliferative activity and may have pharmacokinetic limitations due to its lipophilic character. We report here that cysmethynil can be structurally modified to give analogues that are as potent in inhibiting Icmt but with significantly greater antiproliferative activity. Key modifications were the replacement of the acetamide side chain by tertiary amino groups, the n-octyl side chain by isoprenyl and the 5-m-tolyl ring by fluorine. Moreover, these analogues have lower lipophilicities that could lead to improved pharmacokinetic profiles. © 2010 American Chemical Society.||Source Title:||Journal of Medicinal Chemistry||URI:||http://scholarbank.nus.edu.sg/handle/10635/109921||ISSN:||00222623||DOI:||10.1021/jm1002843|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Sep 24, 2020
WEB OF SCIENCETM
checked on Sep 16, 2020
checked on Sep 26, 2020
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.