TAT peptide immobilization on gold surfaces: a comparison study with a thiolated peptide and alkylthiols using AFM, XPS, and FT-IRRAS.
A TAT peptide was used to functionalize a gold surface by three different methods: adsorption from solution, microcontact printing, and dip-pen nanolithography (DPN). The composition and structure of the modified gold was characterized by atomic force microscopy (AFM), X-ray photoelectron spectroscopy (XPS), and Fourier transform -infrared reflection absorption spectroscopy (FT-IRRAS). We used two well-studied alkylthiols, mercaptohexadecanoic acid and 1-octadecanethiol, as a comparison in order to understand the structure of the TAT peptide monolayers prepared by the three methods. AFM studies allowed us to assess the homogeneity after each modification protocol. XPS was used to characterize the chemical composition of the gold surface after each functionalization procedure. The XPS results showed that surfaces modified with the TAT peptide by the three methods exhibit similar surface chemistry. Finally, FT-IRRAS experiments allowed us to conclude that the structure of the alkyl chains of the TAT peptides is fairly disordered and different after each procedure. Regardless of the type of surface functionalization method used, the monolayer of TAT peptide formed on the surface was of "liquidlike" nature.
Cho
Youngnam
Y
Department of Chemistry, Purdue University, West Lafayette, Indiana 47907, USA.
Ivanisevic
Albena
A
D000327:Adsorption; D015696:Gene Products, tat / Q000493:pharmacokinetics*; D006046:Gold; D018625:Microscopy, Atomic Force; D010455:Peptides / Q000493:pharmacokinetics*; D017550:Spectroscopy, Fourier Transform Infrared; D013438:Sulfhydryl Compounds / Q000493:pharmacokinetics*; D014965:X-Rays
D015696:Gene Products, tat; D010455:Peptides; D013438:Sulfhydryl Compounds; D006046:Gold