Studies on Peptides XVIII. Catalytic Hydrogenation of Methionine-containing Peptides

Yajima, Haruaki; Kawasaki, Koichi; Kinomura, Yasuhiko; Oshima, Takao; Kimoto, Shoshichiro; Okamoto, Masao

doi:10.1248/cpb.16.1342

Cited by 20 publications

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“…The following limitations and disadvantages of these methods can be distinguished as follows: the widely used hydrogenation on a palladium catalyst cannot be applied when the structure contains organic sulfides, including cysteine or methionine residues [ 6 ]. Deblocking can be carried out in the presence of cyclohexylamine or boron trifluoride etherate [ 7 ]. However, the method is not selective in the presence of reducible functional groups such as C=C, C=O, CN, NO 2 , formyl, carbamoyl, etc.…”

Section: Introductionmentioning

confidence: 99%

“…Среди ограничений и недостатков этих методов можно выделить следующие: активно используемый метод гидрирования на палладиевом катализаторе нельзя применить, если в структуре соединения есть органические сульфиды, в том числе остатки цистеина или метионина [6]. Можно проводить деблокирование в присутствии циклогексиламина или эфирата трехфтористого бора [7], однако метод не селективен при наличии восстанавливаемых функциональных групп, таких, как C=C, C=O, CN, NO 2 , формильной, карбамоильной и др. [8].…”

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Specificity of Penicillin Acylases in Deprotection of N-Benzyloxycarbonyl Derivatives of Amino Acids

et al. 2023

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Changes in the structure of the N-acyl group in N-acylated amino acid derivatives significantly affect both the recognition and activity of penicillin acylases on this series of substrates. However, penicillin acylases from both Alcaligenes faecalis and Escherichia coli are capable of removing the N-benzyloxycarbonyl protecting group in amino acid derivatives under mild conditions without the use of toxic reagents. Efficiency in using penicillin acylases in preparative organic synthesis can be improved by utilizing modern rational enzyme design methods.

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Section: Introductionmentioning

confidence: 99%

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Specificity of Penicillin Acylases in Deprotection of N-Benzyloxycarbonyl Derivatives of Amino Acids

et al. 2023

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Conformational properties of methionine homo‐oligopeptides in solution

Bonora

Toniolo

1974

Biopolymers

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SynopsisA conformational analysis was carried out in solution Gn a series of L-methionine oligomers having the general formula BOCfL-Met-f,OMe (n = 2-7). We examined these oligopeptides in TFE, HFIP, EG, and mixed organic-water media. The critical size for helix formation was found to be seven residues in TFE, whereas the @associated structure appears a t the pentamer in EG v/v). In HFIP, however, the oligomers exist essentially in an unordered conformation.

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Co‐oligopeptides of aromatic amino acids and glycine with a variable distance between the aromatic residues. III. Co‐oligopeptides of L‐phenylalanine, L‐tryptophan, and glycine: Synthesis and ultraviolet absorption properties

et al. 1976

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SynopsisThe preparation of the co-oligopeptides of the series H-Gly-Phe-(Gly),-Trp-Gly-OH ( n = 0, 1, 2) and of other free peptides of glycine, L-tryptophan, and L-phenylalanine is reported. The syntheses have been carried out by conventional methods, using N-hydroxysuccinimide esters for the coupling steps. The ultraviolet absorption properties of the free peptides have been investigated in water. No hypo-or hyperchromicity was found for the aromatic chromophores, with the exception of H-Gly-Phe-Trp-OH, which shows a small but significant hypochromicity. The contribution of the peptide bond to the molar absorptivity in the far ultraviolet has been separated from that of the side chain plus the -COO-group by plotting the measured molar absorptivity c of the farthest accessible uv maximum as a function of the number of peptide bonds ( n~) .The peptide bond contribution proved to be independent of n~ in the range n~ = 1-5, thus ruling out the onset of helical conformations in the longer chain peptides.

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Studies on Peptides XVIII. Catalytic Hydrogenation of Methionine-containing Peptides

Cited by 20 publications

References 0 publications

Specificity of Penicillin Acylases in Deprotection of N-Benzyloxycarbonyl Derivatives of Amino Acids

Specificity of Penicillin Acylases in Deprotection of N-Benzyloxycarbonyl Derivatives of Amino Acids

Conformational properties of methionine homo‐oligopeptides in solution

Co‐oligopeptides of aromatic amino acids and glycine with a variable distance between the aromatic residues. III. Co‐oligopeptides of L‐phenylalanine, L‐tryptophan, and glycine: Synthesis and ultraviolet absorption properties

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