1026257-87-3Relevant academic research and scientific papers
Hafnium-catalyzed direct amide formation at room temperature
Lundberg, Helena,Adolfsson, Hans
, p. 3271 - 3277 (2015)
Herein, the first example of a metal-catalyzed protocol for direct amidation of nonactivated carboxylic acids at ambient temperature (26 °C) is presented. The mild reaction conditions give rise to high yields of a range of amides in reaction times as short as 90 min, employing a commercial hafnium complex, [Hf(Cp)2Cl2], as catalyst. Amino acids are transformed into their corresponding amides without racemization, and the catalyst displays full selectivity for the amidation of carboxylic acids over esters. Electronic properties of the carboxylic acids were found to have a strong influence on the rate of the amidation reaction, and the need for a balanced amount of molecular sieves was observed to be highly important for optimal reaction outcome.
Pseudodipeptide Inhibitors of Protein Farnesyltransferase
de Solms, S. Jane,Deana, Albert A.,Giuliani, Elizabeth A.,Graham, Samuel L.,Kohl, Nancy E.,et al.
, p. 3967 - 3971 (2007/10/03)
A series of pseudodipeptide amides are described that inhibit Ras protein farnesyltransferase (PFTase).These inhibitors are truncated versions of the C-terminal tetrapeptide (CAAX motif) of Ras that serves as the signal sequence for PFTase-catalyzed protein farnesylation.In contrast to CAAX peptidomimetics previously reported, these inhibitors do not have a C-terminal carboxyl moiety, yet they inhibit farnesylation in vitro at 100 nM.Despite the absence of the X residue in the CAAX motif, which normally directs prenylation specificity, these pseudodipeptides are greater than 100-fold selective for PFTase over type 1 protein geranylgeranyltransferase.
