## 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,
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
✍ Scribed by Rocco Guarnaccia; Gian Paolo Lorenzi; Vincenzo Rizzo; Pier Luigi Luisi
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1975
- Tongue
- English
- Weight
- 851 KB
- Volume
- 14
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
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‐hydroxysuccinimide esters for the coupling steps. All the oligopeptides were obtained after purfication as colorless and crystalline products, and gave only one spot on thin‐layer chromatography. Specfic problems connected with the synthesis and purficiation of optically pure tryptophan‐containing peptides are discussed.
📜 SIMILAR VOLUMES
## 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.
## 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
## 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 cou
## 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