作者: Edoardo Longo , Karen Wright , Mario Caruso , Emanuela Gatto , Antonio Palleschi
DOI: 10.1039/C5NR03549J
关键词: Peptide sequence 、 Scanning tunneling microscope 、 Chronoamperometry 、 Cyclic voltammetry 、 Population 、 Stereochemistry 、 Electron transfer 、 Crystallography 、 X-ray photoelectron spectroscopy 、 Chemistry 、 Peptide
摘要: A helical hexapeptide was designed to link in a rigid parallel orientation gold surface. The peptide sequence of the newly synthesized compound is characterized by presence two 4-amino-1,2-dithiolane-4-carboxylic acid (Adt) residues (positions 1 and 4) promote bidentate interaction with surface, L-Ala 2 5) two-aminoisobutyric (Aib) 3 6) favor high population 310-helix conformation. Furthermore, ferrocenoyl (Fc) probe inserted at N-terminus investigate electronic conduction properties peptide. X-Ray photoelectron spectroscopy scanning tunneling microscopy techniques were used characterize binding surface morphology layer, respectively. Several electrochemical (cyclic voltammetry, chronoamperometry, square wave voltammetry) applied analyze activity Fc probe, along influence 3D-structure layer on electron transfer processes.