Thiazole–amino acids: influence of thiazole ring on conformational properties of amino acid residues
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F21%3A00542031" target="_blank" >RIV/61388963:_____/21:00542031 - isvavai.cz</a>
Výsledek na webu
<a href="https://doi.org/10.1007/s00726-021-02974-0" target="_blank" >https://doi.org/10.1007/s00726-021-02974-0</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s00726-021-02974-0" target="_blank" >10.1007/s00726-021-02974-0</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Thiazole–amino acids: influence of thiazole ring on conformational properties of amino acid residues
Popis výsledku v původním jazyce
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.
Název v anglickém jazyce
Thiazole–amino acids: influence of thiazole ring on conformational properties of amino acid residues
Popis výsledku anglicky
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.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10403 - Physical chemistry
Návaznosti výsledku
Projekt
—
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2021
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Amino Acids
ISSN
0939-4451
e-ISSN
1438-2199
Svazek periodika
53
Číslo periodika v rámci svazku
5
Stát vydavatele periodika
AT - Rakouská republika
Počet stran výsledku
14
Strana od-do
673-686
Kód UT WoS článku
000638833600001
EID výsledku v databázi Scopus
2-s2.0-85104241621