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

✍ Scribed by Robert Saltman; Dagmar Vlach; Pier Luigi Luisi

Publisher
Wiley (John Wiley & Sons)
Year
1977
Tongue
English
Weight
476 KB
Volume
16
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

Several N‐protected peptide amides, containing two aromatic residues spaced by one glycyl residue, have been enzymatically synthesized starting from P‐Ar‐OH and H‐Gly‐Ar‐NH~2~ (P is the protecting group and Ar is the aromatic residue) and using α‐chymotrypsin as the catalyst for the coupling step. Reactions have been carried out in water solution, at room temperature, and afford yields ranging between 20 and 75% ca. This coupling reaction occurs in a much more restricted set of conditions than the hydrolysis reaction, e.g., only within a small pH range (ca. 6.5–7.5) and with particular buffering agents. The advantages and limitations of this type of reaction, compared with conventional coupling procedures, are discussed.

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Co-oligopeptides of aromatic amino acids
Co-oligopeptides of aromatic amino acids and glycine with a variable distance between the aromatic residues. I. Synthesis of co-oligopeptides of tryptophan and glycine
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## Abstract The preparation of the co‐oligopeptides of the series H‐Gly‐Trp‐(Gly)~__n__~‐Trp‐Gly‐OH (__n__ = 0, 1, and 2) and of a number of other unprotected co‐oligopeptides of glycine and tryptophan is reported. The syntheses have been carried out by conventional methods, using, in general, __N_

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## Abstract The uv absorption and circular dichroism (CD) properties in water (pH 5.9) and trifluoroethanol of several co‐oligopeptides of glycine and tryptophan have been investigated. These compounds contain one tryptophyl residue, such as H‐Gly‐Trp‐OH, H‐Trp‐Gly‐OH, and H‐Gly‐Trp‐Gly‐OH; or two,

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## Abstract The preparation of the co‐oligopeptides of the series H‐Gly‐Phe‐(Gly)~__n__~‐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 est

Co-oligopeptides of aromatic amino acids
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## Abstract The circular dichroic properties of H‐Gly‐Phe‐(Gly)~__n__~‐Trp‐Gly‐OH (II, __n__ = 0,1,2) and of related simpler peptides, such as H‐Phe‐Gly‐OH, H‐Gly‐Phe‐OH, H‐Gly‐Phe‐Gly‐OH, H‐Phe‐Trp‐OH, H‐Phe‐Trp‐Gly‐OH, and H‐Gly‐Phe‐Trp‐OH in water and trifluoroethanol solutions are investigated.

Co-oligopeptides of aromatic amino acids
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## Abstract The influence of pH upon CD spectra of H‐Trp‐Trp‐OH, H‐Trp‐Trp‐Gly‐OH, and H‐Gly‐Trp‐Trp‐OH is investigated and data are compared with those obtained for peptides containing only one tryptophyl residue. A negative Cotton effect at around 225 nm, which in previous work has been related t