355121-59-4Relevant academic research and scientific papers
CALPAIN MODULATORS AND THERAPEUTIC USES THEREOF BACKGROUND
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Paragraph 0235; 0238, (2019/11/28)
Disclosed herein are small molecule calpain modulators, pharmaceutical compositions, preparation methods and their use as therapeutic agents. The therapeutic agents can be used for treating fibrotic disease or a resulting secondary disease state or condition. The small molecules can inhibit calpain through contact with CAPN1, CAPN2, and/or CAPN9 enzymes.
A mild ligand-free iron-catalyzed liberation of alcohols from allylcarbonates
Dieskau, Andre P.,Plietker, Bernd
, p. 5544 - 5547 (2011/12/05)
Different from most carbonates the allyloxy carbonyl protecting group can be cleaved under neutral conditions using metal catalysis. However, most of the catalysts employed to date are based upon precious metals. Herein we present two protocols for the mild Fe-catalyzed liberation of alcohols from allylcarbonates that are characterized by broad functional group tolerance and exclusive chemoselectivity.
Large scale synthesis of the Cdc42 inhibitor secramine A and its inhibition of cell spreading
Xu, Bo,Pelish, Henry,Kirchhausen, Tomas,Hammond, Gerald B.
, p. 4149 - 4157 (2008/09/19)
We describe a large scale synthesis of secramine A. Consistent with its ability to inhibit activation of the small GTPase Cdc42, we find that secramine A inhibits cell spreading, a process previously shown to be Cdc42-dependent. The Royal Society of Chemistry 2006.
An improved solid-phase methodology for the synthesis of putative hexa- and heptapeptide intermediates in vancomycin biosynthesis
Li, Dong Bo,Robinson, John A.
, p. 1233 - 1239 (2007/10/03)
The biosynthesis of the vancomycin aglycone involves three oxidative phenol coupling reactions, each catalyzed by a discrete cytochrome P450-like enzyme. Studies on the mechanism and specificity of the enzyme (called OxyB) catalyzing the first coupling, require access to suitable linear peptide precursors, each conjugated as a thioester to a peptide carrier domain of the vancomycin non-ribosomal peptide synthetase. An efficient route to representative free linear peptides is described here. The method makes use of Alloc-chemistry during solid-phase assembly of the peptide backbone, but importantly and in contrast to earlier efforts, largely avoids the use of amino acid side chain protecting groups. In this way, the target linear peptides can be released directly from the solid support under very mild conditions. The Royal Society of Chemistry 2005.
