Co‐oligopeptides of aromatic amino acids and glycine with variable distance between the aromatic residues. VII. Enzymatic synthesis of N‐protected peptide amides

Saltman, Robert; Vlach, D.; Luisi, Pier Luigi

doi:10.1002/bip.1977.360160312

Cited by 31 publications

(9 citation statements)

References 17 publications

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“…This process was found to be specific for the L-isomer of the esters, a fact that should make it possible to use racemic starting material. Based on published results with endoprotease catalyzed condensation of peptide fragments (9,11,12,13,18), it may become possible to isolate individual oligomeric fragments and couple them to produce monodisperse, optically pure poly-a-amino acids of predetermined size.…”

Section: Discussionmentioning

confidence: 99%

Carboxypeptidase Y catalyzed peptide synthesis using amino acid alkyl esters as amine components

Widmer

Breddam

Johansen

1980

Carlsberg Res. Commun.

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Carboxypeptidase Y catalyzed transacylation reactions between N-protected amino acid methyl esters or peptide methyl esters as initial acyl components and methyl, ethyl, isopropyl or tert.-butyl esters of different aamino acids as amine components are described. The yield of peptide bond formation and the extent of oligomerization of the amine components both depend on the nature of their side chain as well as on the nature of their alkyl ester group. Thus, the methyl esters of all hydrophobic amino acids that were tested oligomerized to various extents (in total product yields ranging from 60-90 %). On the other hand, the methyl esters of the hydrophilic amino acids did not oligomerize, and were incorporated in yields ranging from 25-50 %. Increasing the size of the ester group from methyl, to ethyl, to propyl etc. resulted in a drastic decrease of the degree of oligomerization and -with the exception of glycine -led to reduced coupling yields.

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Section: Discussionmentioning

confidence: 99%

Carboxypeptidase Y catalyzed peptide synthesis using amino acid alkyl esters as amine components

Widmer

Breddam

Johansen

1980

Carlsberg Res. Commun.

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“…Interestingly, chymotrypsin was effective in the synthesis of some Boc-derivatives, Boc-Tyr-Gly-Tyr-NH2 and Boc-Phe-Gly-Phe-NH2, for example. 2 One of the main advantages of enzymatic syntheses lies in the optical purity of the products. This has two interesting aspects.…”

Section: Resultsmentioning

confidence: 99%

Pepsin‐catalyzed peptide synthesis

Pellegrini

Luigilusis

1978

Biopolymers

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SynopsisThe use of pepsin as a catalyst for the synthesis of peptide bonds was investigated. It is shown that the enzyme enables the preparation of several protected dipeptides and tripeptides containing two adjacent aromatic residues of the type P-Al-Phe-Phe-Y, P-Phe-Ar-Y, or P-AR-Phe-Y where P and Yare amino and carboxyl protecting groups, A1 is an aliphatic amino acid residue, and Ar is an aromatic, amino acid residue. The yields are in the range 25-97%,. The high yields, combined with the enzyme's stereospecificity, permit the isolation of optically pure enantiomers from racemic mixtures. For example, when Z-DL-Phe-OH is allowed to react with an excess of H -L -P~~-N H~, the stereoisomer z -~-P h e -~-P h e -N H z is obtained in practically quantitative yield. At the same time, the unreacted, optically pure Z-D-Phe-OH can be recovered (Z = carbobenzyloxy, Phe = phenylalanine). The advantages and disadvantages of the enzymatic coupling procedure as a possible routine method for peptide synthesis are discussed.

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“…The results of Oka and Morihara (178) may be compared with those of Luisi et al (9,179), who examined the condensation of Z-Trp-OH, BocTrp-OH, Z-Tyr-OH, Z-Phe-OH, or Boc-Phe-OH (concentration undefined) with several peptide amides (at equimolar concentrations) and amino acid esters (in excess) at pH 7.7. After 2-5 days at room temperature, the highest yields (75%) of precipitated product were obtained in the condensation of Z-Tyr-OH with H-Gly-Tyr-NHz and of Z-Phe-OH with H-Gly-Phe-OH (9).…”

Section: B Chymotrypsinmentioning

confidence: 99%

“…After 2-5 days at room temperature, the highest yields (75%) of precipitated product were obtained in the condensation of Z-Tyr-OH with H-Gly-Tyr-NHz and of Z-Phe-OH with H-Gly-Phe-OH (9). No account was taken of the possible diketopiperazine formation from these dipeptide amides during the long incubation period.…”

Section: B Chymotrypsinmentioning

confidence: 99%

“…For this reason, the recent efforts to use proteinases as specific reagents in the assembly of peptide chains (5) merit attention, and encouragement may be drawn from the valuable contributions of Inouye and his colleagues on the condensation of protected fragments of human insulin by means of pancreatic trypsin (6). Moreover, the enzymatic methods have been used in the synthesis of smaller biologically active peptides, such as angiotensin I1 and enkephalin (7,8), and of oligopeptides needed for physicochemical studies (9).…”

Section: Introductionmentioning

confidence: 99%

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