6173-77-9Relevant academic research and scientific papers
Novel synthesis of various orthogonally protected Cα- methyllysine analogues and biological evaluation of a Vapreotide analogue containing (S)-α-methyllysine
Banerjee, Souvik,Wiggins, Walker J.,Geoghegan, Jessie L.,Anthony, Catherine T.,Woltering, Eugene A.,Masterson, Douglas S.
, p. 6307 - 6319 (2013/09/23)
Prochiral malonic diesters containing a quaternary carbon center have been successfully transformed into a diverse set of tBoc-Fmoc- α2,2-methyllysine-OH analogues through chiral malonic half-ester intermediates obtained via enzymatic (Pig Liver Esterase, PLE) hydrolysis. The variety of chiral half-ester intermediates, which vary from 1 to 6 methylene units in the side chain, are achieved in moderate to high optical purity and in good yields. The PLE hydrolysis of malonic diesters with various side chain lengths appears to obey the Jones's PLE model according to the stereochemical configurations of the resulting chiral half-esters. The established synthetic strategy allows the construction of both enantiomers of α2,2-methyllysine analogues, and a (S)-β2,2- methyllysine analogue from a common synthon by straightforward manipulation of protecting groups. Two different straightforward and cost effective synthetic strategies are described for the synthesis of α2,2-methyllysine analogues. The described strategies should find significant usefulness in preparing novel peptide libraries with unnatural lysine analogues. A Vapreotide analogue incorporating (S)-α2,2-methyllysine was prepared. However, the Vapreotide analogue with (S)-α-methyl-α-lysine is found to lose its specific binding to somatostatin receptor subtype 2 (SSTR2).
Stereospecific construction of chiral quaternary carbon compounds from chiral secondary alcohol derivatives
Masaki, Yukio,Arasaki, Hideki,Iwata, Masashi
, p. 4 - 5 (2007/10/03)
Chiral tertiary dichloromethylcarbinol derivatives, prepared by stereospecific α C-H insertion reaction of dichlorocarbene with protected chiral secondary alcohols, were converted into intermediary α-chloroepoxides which gave stereospecifically chiral qua
Enzymatic resolution of α,α-disubstituted α-amino acid esters and amides
Kaptein,Boesten,Broxterman,Peters,Schoemaker,Kamphuis
, p. 1113 - 1116 (2007/10/02)
The scope and limitations of the enzymatic resolution of α,α-disubstituted α-amino acid amides by an amino acid amidase from Mycobacterium neoaurum and of the corresponding ethyl esters with Pig liver esterase (PLE) have been studied. Moderate enantiomeric excesses were obtained with PLE, with only a narrow substrate specificity. Mycobacterium neoaurum on the contrary yields a broad range of S-α,α-disubstituted α-amino acids 1 and the corresponding R-amides 2.
