6533b837fe1ef96bd12a1d4f
RESEARCH PRODUCT
Thiazole–amino acids: influence of thiazole ring on conformational properties of amino acid residues
Małgorzata A. BrodaMonika StaśDawid Siodłaksubject
0301 basic medicineStereochemistryClinical BiochemistryNon-standard amino acidsMolecular ConformationRamachandran map010402 general chemistryRing (chemistry)01 natural sciencesBiochemistryDFT03 medical and health scienceschemistry.chemical_compoundDehydroalanineAmino AcidsStructural motifThiazoleOxazoleAlaninechemistry.chemical_classificationHydrogen bondNon-standard amino AIDSHydrogen bondOrganic ChemistryHydrogen Bonding0104 chemical sciencesAmino acidThiazoles030104 developmental biologyConformational analysischemistryOriginal ArticleThiazolePeptidesdescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2021-04-01 | Amino Acids |