β-Turn structure in glycinylphenylalanine dipeptide based N-amidothioureas

• DOI: 10.1039/c3cc44336a
• Publication Date: 2013-08-06T08:38:23Z
• Authors: Xiao-Sheng Yan; Kun Wu; Yuan Yuan; Ying Zhan; Jin-He Wang; Zhao Li; Yun-Bao Jiang
• Keywords: RESIDUE; SCAFFOLD; Circular Dichroism; PREFERENCE; Thiourea; PROTEIN; Hydrogen Bonding; AZAPEPTIDES; Dipeptides; Amides; 01 natural sciences; Protein Structure, Secondary; 3. Good health; 0104 chemical sciences; CHIRALITY; PEPTIDE

Transforming the C-terminal amide of a glycinylphenylalanine dipeptide into N-amidothiourea affords a β-turn structure in the formed dipeptide based N-amidothioureas, which can be readily identified by an induced CD signal from the achiral phenylthiourea chromophore.