29582-96-5Relevant academic research and scientific papers
Anthranilimide-based glycogen phosphorylase inhibitors for the treatment of Type 2 diabetes: 2. Optimization of serine and threonine ether amino acid residues
Sparks, Steven M.,Banker, Pierette,Bickett, David M.,Clancy, Daphne C.,Dickerson, Scott H.,Garrido, Dulce M.,Golden, Pamela L.,Peat, Andrew J.,Sheckler, Lauren R.,Tavares, Francis X.,Thomson, Stephen A.,Weiel, James E.
scheme or table, p. 981 - 985 (2009/08/15)
Optimization of the amino acid residue of a series of anthranilimide-based glycogen phosphorylase inhibitors is described leading to the identification of serine and threonine ether analogs. t-Butylthreonine analog 20 displayed potent in vitro inhibition of GPa, low potential for P450 inhibition, and excellent pharmacokinetic properties.
Chemo-enzymatic synthesis of optically active amino acids and peptides
Chen, Shui-Tein,Wang, Kung-Tsung
, p. 301 - 311 (2007/10/03)
The industrial alkaline protease, alcalase, is stable and active in a high concentration of organic solvents and useful as a biocatalyst for (i) diastereoselective hydrolysis of peptide esters and preparation of racemization-free peptides; (ii) selective incorporation of esters of D-amino acid into peptides in t-butanol via a selective hydrolysis of esters of D,L-amino acid, followed by using the unhydrolyzed D-esters as a nucleophile in a kinetically controlled peptide bond formation; (iii) resolution of esters of amino acid in 95% t-butanol/5% water, followed by saponification of the unreacted esters to offer both enantiomers with high yield and optical purity; (iv) completely resolve amino-acid esters with high yield and optical purity via in situ racemization of the unreacted antipode catalyzed by pyridoxal 5-phosphate; (v) cryobioorganic synthesis of peptides with increased yields 15%-40% of peptide bond formation by reaction at 5 °C instead of 25-30 °C of a kinetically controlled enzymatic reaction in alcohols.
