16-mercaptohexadecanoic-acid and gallium-arsenide

Wet chemical processes were investigated to remove alkanethiol self-assembled monolayers (SAMs) and regenerate GaAs (001) samples studied in the context of the development of reusable devices for biosensing applications. The authors focused on 16-mercaptohexadecanoic acid (MHDA) SAMs that are commonly used to produce an interface between antibodies or others proteins and metallic or semiconductor substrates. As determined by Fourier transform infrared absorption spectroscopy, among the investigated solutions of HCl, H2O2, and NH4OH, the highest efficiency in removing alkanethiol SAM from GaAs was shown by NH4OH:H2O2 (3:1 volume ratio) diluted in H2O. The authors observed that this result was related to chemical etching of GaAs that even in a weak solution of NH4OH:H2O2:H2O (3:1:100) proceeded at a rate of 130 nm/min. The surface revealed by a 2-min etching under these conditions allowed depositing successfully a new MHDA SAM with comparable quality and density to the initial coating. This work provides an important view on the perspective of the development of a family of cost-effective GaAs-based biosensors designed for repetitive detection of a variety of biomolecules immobilized with dedicated antibody architectures.

Topics: Antibodies; Arsenicals; Chemical Phenomena; Electrolytes; Gallium; Palmitic Acids; Protein Binding; Solvents; Spectroscopy, Fourier Transform Infrared; Surface Properties

Four TAT peptide fragments were used to functionalize GaAs surfaces by adsorption from solution. In addition, two well-studied alkylthiols, mercaptohexadecanoic acid (MHA) and 1-octadecanethiol (ODT) were utilized as references to understand the structure of the TAT peptide monolayer on GaAs. The different sequences of TAT peptides were employed in recognition experiments where a synthetic RNA sequence was tested to verify the specific interaction with the TAT peptide. The modified GaAs surfaces were characterized by atomic force microscopy (AFM), X-ray photoelectron spectroscopy (XPS), and Fourier transform infrared reflection absorption spectroscopy (FT-IRRAS). AFM studies were used to compare the surface roughness before and after functionalization. XPS allowed us to characterize the chemical composition of the GaAs surface and conclude that the monolayers composed of different sequences of peptides have similar surface chemistries. Finally, FT-IRRAS experiments enabled us to deduce that the TAT peptide monolayers have a fairly ordered and densely packed alkyl chain structure. The recognition experiments showed preferred interaction of the RNA sequence toward peptides with high arginine content.

Topics: Arginine; Arsenicals; Gallium; Gene Products, tat; Microscopy, Atomic Force; Palmitic Acids; Peptide Fragments; RNA; Spectroscopy, Fourier Transform Infrared; Sulfhydryl Compounds; Surface Properties; X-Rays