36992-14-0Relevant articles and documents
Biocatalyzed kinetic resolution of racemic mixtures of chiral α-aminophosphonic acids
Kozyra, Kinga,Brzezinska-Rodak, Malgorzata,Klimek-Ochab, Magdalena,Zymanczyk-Duda, Ewa
, p. 32 - 36 (2013)
Several fungal species namely: Aspergillus niger, Aspergillus parasiticus, Penicillium funiculosum, Trigonopsis variabilis and two different strains of Fusarium oxysporum were tested toward racemic mixtures of following phosphonic acids: 1-amino-2-methylp
Penicillin G acylase-mediated kinetic resolution of racemic 1-(N-acylamino)alkylphosphonic and 1-(N-acylamino)alkylphosphinic acids and their esters
Zielińska, Katarzyna,Mazurkiewicz, Roman,Szymańska, Katarzyna,Jarz?bski, Andrzej,Magiera, Sylwia,Erfurt, Karol
, p. 31 - 40 (2016/07/19)
Extensive studies on the penicillin G acylase-mediated kinetic resolution of N-acylated 1-aminoalkylphosphonic and 1-aminoalkylphosphinic acids as well as their esters were carried out to recognise the relationships between the substrate structure, reacti
Synthesis of five enantiomerically pure haptens designed for in vitro evolution of antibodies with peptidase activity
Wagner, Juergen,Lerner, Richard A.,Barbas III, Carlos F.
, p. 901 - 916 (2007/10/03)
A series of five haptens have been synthesized for use in in vitro selection experiments from combinatorial antibody libraries. Haptens were designed for the recruitment of serine and cysteine pretense reaction mechanisms for the cleavage of Phe-Ala and Phe-Phe (L,L) dipeptide analogues. For the selection of transition state stabilization, Phe(P)(O)Ala (7) and PheP(O)Phe (10) derivatives were synthesized using the Mitsunobu approach where Phe(P) represents the phosphonic acid analogue of phenylalanine and (O)Phe and (O)Ala represent (L)-β-phenyllactic and (L)-lactic acid, respectively. Optically pure peptidyl diazomethyl ketones 16 and 22 were synthesized for selection of the catalytic ensemble of cysteine proteases. An optically pure dipeptidyl boronic acid 26 was synthesized for the selection of the catalytic ensemble of serine proteases. A strategy for the evolution el catalytic antibodies using these haptens was developed which includes mechanism-based selections. Since mechanism based selections result in covalent trapping of species from libraries, diol and disulfide containing haptenic linkers were developed for the oxidative or reductive release of selected catalysts.