Unknown

Dataset Information

0

Thiazole-amino acids: influence of thiazole ring on conformational properties of amino acid residues.


ABSTRACT: Post-translational modified thiazole-amino acid (Xaa-Tzl) residues have been found in macrocyclic peptides (e.g., thiopeptides and cyanobactins), which mostly inhibit protein synthesis in Gram + bacteria. Conformational study of the series of model compounds containing this structural motif with alanine, dehydroalanine, dehydrobutyrine and dehydrophenylalanine were performed using DFT method in various environments. The solid-state crystal structure conformations of thiazole-amino acid residues retrieved from the Cambridge Structural Database were also analysed. The studied structural units tend to adopt the unique semi-extended β2 conformation; which is stabilised mainly by N-H⋯NTzl hydrogen bond, and for dehydroamino acids also by π-electron conjugation. The conformational preferences of amino acids with a thiazole ring were compared with oxazole analogues and the role of the sulfur atom in stabilising the conformations of studied peptides was discussed.

SUBMITTER: Stas M 

PROVIDER: S-EPMC8128816 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC4122135 | biostudies-literature
| S-EPMC6299098 | biostudies-literature
| S-EPMC7394324 | biostudies-literature
| S-EPMC7438526 | biostudies-literature
| S-EPMC22969 | biostudies-literature
| S-EPMC5274556 | biostudies-literature
| S-EPMC9860158 | biostudies-literature
| S-EPMC4718141 | biostudies-literature
| S-EPMC6255834 | biostudies-literature
| S-EPMC9496368 | biostudies-literature