Elucidation of the Conformation of Polyglycine Organo-Polyoxotungstates: Evidence for Zipper Folding

作者：Vilona Debora; Lachkar David; Dumont Elise^*; Lelli Moreno^*; Lacote Emmanuel^*

来源：Chemistry - A European Journal, 2017, 23(54): 13323-13327.

DOI：10.1002/chem.201703509

• hydrogen bonds
• molecular dynamics
• molecular modeling
• peptides
• polyoxometalates

The conformation of a family of alpha(1) and alpha(2) polyglycine-containing organo-polyoxometalates was determined through a mixed experimental/molecular dynamics approach. The flexible peptide arm folds around the metal oxide surface in a rigid arrangement in low to average polarity solvents. The topology of the hybrid is the main factor that determines which oxos from the metal-oxide surface accept a H-bond from the closest amino acid. The rest of the peptide follows in a zipper mechanism that establishes a H-bond network that locks the system. The covalent constraint leads to a new type of H-bond where two consecutive amino acids clamp down terminal oxo ligands.

• 出版日期2017-9-27
• 单位河南工业大学