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

0542031 - ÚOCHB 2022 RIV AT eng J - Journal Article
Staś, Monika - Broda, M. A. - Siodłak, D.
Thiazole–amino acids: influence of thiazole ring on conformational properties of amino acid residues.
Amino Acids. Roč. 53, č. 5 (2021), s. 673-686. ISSN 0939-4451. E-ISSN 1438-2199
Institutional support: RVO:61388963
Keywords : thiazole * non-standard amino acids * conformational analysis * Ramachandran map * hydrogen bond * DFT
OECD category: Physical chemistry
Impact factor: 3.789, year: 2021
Method of publishing: Open access
https://doi.org/10.1007/s00726-021-02974-0

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.
Permanent Link: http://hdl.handle.net/11104/0319526