Electronic transport in a graphene single layer: application in amino acid sensing.

We modeled a type of field-effect transistor device based on graphene for the recognition of amino acids with a potential application in the building of a protein sequencer. The theoretical model used was a combination of density functional theory (DFT) with the non-equilibrium Green's function (NEGF) in order to describe the coherent transport in molecular devices. First, we studied the physisorption of each amino acid on a graphene sheet and we reported the adsorption energy, the adsorption distances, the equilibrium configuration and the charge transfer of ten amino acids that can be considered as representative of all of the amino acids: histidine (His), alanine (Ala), aspartic acid (Asp), tyrosine (Tyr), arginine (Arg), glutamic acid (Glu), glycine (Gly), phenylalanine (Phe), proline (Pro) and lysine (Lys). As a result, significant differences were found in the density of states (DOS) after adsorption and there was a change in the semi-metallic character of the graphene due to the lysine and arginine interactions. Furthermore, we noticed changes in the electrical characteristics of the devices, as the amino acids adsorbed onto the surface of the graphene. The curves of current vs. bias voltage (I-Vb) display a distinct response for each amino acid, i.e. the I-Vb curves produce a characteristic footprint for each amino acid. We identified a possible rectification mechanism related to the voltage profile asymmetry, where the amino acids can control the transport characteristics in the device, i.e. Lys and Phe amino acids physisorbed on graphene act as a molecular diode, where electrons can easily flow in one direction and decrease in the other. This may be promising for the prospect of biosensors: graphene could be used as an amino acid detector.

Sequencing of argentinated peptides by means of matrix-assisted laser desorption/ionization tandem mass spectrometry.

Argentinated peptide ions are formed in abundance under matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) conditions in the presence of Ag+ ions. These argentinated peptide ions are fragmented facilely under MALDI-MS/MS conditions to yield [b(n) + OH + Ag]+, [b(n) - H + Ag]+ and [a(n) - H + Ag]+ ions that are indicative of the C-terminal sequence. These observations parallel those made earlier under electrospray MS conditions (Chu, I. K; Guo, X.; Lau, T.-C.; Siu, K W. M. Anal. Chem. 1999, 71, 2364-2372). A mixed protonated and argentinated tryptic peptide map was generated from 37 fmol of bovine serum albumin (BSA) using MALDI-MS. MALDI-MS/MS data from four argentinated peptides at a protein amount of 350 fmol unambiguously identified the protein as BSA. Sequence-tag analysis of two argentinated tryptic peptides was used to identify unambiguously myocyte enhancer factor 2A, which had been recombinantly expressed in a bacterial cell line.