Portal de Periódicos da CAPES

Lipase-catalyzed synthesis of peptides containing d-amino acid

1998; Elsevier BV; Volume: 23; Issue: 3-4 Linguagem: Inglês

10.1016/s0141-0229(98)00051-9

1879-0909

Jin-Eon So, Seunghyun Kang, Byung‐Gee Kim,

Carbohydrate Chemistry and Synthesis

The lipase-catalyzed synthesis of various dipeptides containing d-amino acid was studied. Lipase from porcine pancreas (PPL) was the only lipase which catalyzed the synthesis of Bz-Tyr-d-Ala-NH2 from Bz-l-Tyr-OEt and H-d-Ala-NH2. Peptide yields reached 90% in 3-methyl-3-pentanol containing 5% (v/v) buffer. To examine the S1 and S′1 site specificity of PPL, the syntheses of Bz-l-Tyr-d-aa-X and X-l-aa-d-Ala-NH2 were performed separately. The results are summarized as follows: 1. Among various kinds of d-amino acid derivatives, H-d-Ala-NH2, H-d-Ser-OMe, H-d-Thr-OMe, H-d-His-OMe, and β-Ala-OMe are good acyl acceptors; 2. l-isomers of the above d-amino acids show similar reactivity for peptide synthesis, but corresponding d-isomers result in better yields; 3. In the case of histidine, only d-isomer displays S′1 site substrate specificity; and 4. Besides Bz-l-Tyr-OEt, the n-protected α-carboxy ester of l-Ala, l-Arg, l-His, l-Trp, and l-Phe can be used as an acyl donor.