a-Trifluoromethyl a-amino acids are potentially intaresting candidates for modification of biological active peptides. We report on new strategies for asymmetric synthesis of a-trifluoromethyl substituted a-amino acids. Approaches to amino group protection and carboxylic group activation are present
Incorporation of Cα-methyl amino acids by solid phase peptide synthesis in a peptide sequence
✍ Scribed by Alié Brunissen; Mimoun Ayoub; Solange Lavielle
- Publisher
- Elsevier Science
- Year
- 1996
- Tongue
- French
- Weight
- 264 KB
- Volume
- 37
- Category
- Article
- ISSN
- 0040-4039
No coin nor oath required. For personal study only.
✦ Synopsis
S)-ctMethyimethionine, (S)-ctMethylleucine, 2-aminoisobutyric acid and (S)-otMethylphenylalanine have been incorporated by solid phase peptide strategy in a peptide sequence.
The coupling reactions of these Boc-ctMe amino acids and of the following residue in the sequence were readily achieved after silylation with chlorotrimethylsilane of the amine function on the resin.
📜 SIMILAR VOLUMES
## Abstract The crystal‐state conformations of three protected tripeptides, four tetrapeptides, and one pentapeptide, heavily based on the chiral C^α^‐methylated α‐amino acids Iva, (αMe)Nva, and (Me)Val, were assessed by X‐ray diffraction analyses. The eight peptide sequences are as follows: Z(DI
A new strategy for solid-phase synthesis of C-terminal peptide amides based on the use of N-tetrachlorophthaloyl protected amino acids with acid-labile side-chain protection is described.
The utility of benzoyl and pentadeuterobenzoyl derivatives of peptide methyl esters for mass spectrometric analysis was investigated. The mass spectra of the glu-his and the Val-tyr-pro derivatives are discussed. Treatment of the peptide methyl esters with the mixed benzoic-ethylcarbonic anhydride d