15891-49-3Relevant articles and documents
General Access to Modified α-Amino Acids by Bioinspired Stereoselective γ-C?H Bond Lactonization
Vicens, Laia,Bietti, Massimo,Costas, Miquel
supporting information, p. 4740 - 4746 (2020/12/25)
α-Amino acids represent a valuable class of natural products employed as building blocks in biological and chemical synthesis. Because of the limited number of natural amino acids available, and of their widespread application in proteomics, diagnosis, drug delivery and catalysis, there is an increasing demand for the development of procedures for the preparation of modified analogues. Herein, we show that the use of bioinspired manganese catalysts and H2O2 under mild conditions, provides access to modified α-amino acids via γ-C?H bond lactonization. The system can efficiently target 1°, 2° and 3° γ-C?H bonds of α-substituted and achiral α,α-disubstituted α-amino acids with outstanding site-selectivity, good to excellent diastereoselectivity and (where applicable) enantioselectivity. This methodology may be considered alternative to well-established organometallic procedures.
Pronase catalysed peptide syntheses
Lobell, Mario,Schneider, Manfred P.
, p. 319 - 325 (2007/10/03)
A mixture of proteases from Streptomyces griseus (pronase), displaying a very broad substrate tolerance in the hydrolysis of peptides, has been studied for the first time systematically regarding their substrate specificity in peptide synthesis. It is demonstrated that pronase can be employed successfully for the formation of dipeptides with yields up to 95%. Pronase has also been employed successfully as catalyst for the enzyme assisted synthesis of a hexapeptide.
