Printed biomolecular templates for 2D material patterning

Abstract

An approach for printing micron-scale electronic devices built from two-dimensional materials is presented. Experimental phage display techniques and computational atomistic simulation approaches were used to identify a peptide molecule that effectively anchors to the basal plane surface of two-dimensional (2D) MoS2 to SiO2 surfaces. This peptide was suspended in water to develop an ink suitable for aerosol jet printing. The printed substrates were then dip coated with a suspension of liquid phase exfoliated 2D MoS2 particles. Strong adhesion of physically continuous lines of these particles was observed only on regions of the substrate patterned with the peptide-based ink, thereby enabling aerosol jet printing as a template for devices based on 2D materials. Graphene was also bound to SiO2 via a similar approach, but with a different peptide known from prior work to selectively adhere to the basal plane of graphene. Fundamental peptide-surface interactions for MoS2, graphene, and SiO2 were explored via simulation and experiment. This printing method is proposed as a route towards large-scale, low temperature patterning of 2D materials and devices. The electrical properties of continuous lines of MoS2 particles printed in a single pass of peptide ink printing were measured via transmission line measurements. The results indicate that this molecular attachment approach to printing possesses several advantages such as overcoming nozzle clogging due to nanomaterial aggregation, decoupling of particle size from any dimensions associated with the printer, and single-pass printing of electrically continuous films.

Interpretable molecular models for molybdenum disulfide and insight into selective peptide recognition

“…[4][5][6][7][8][9][10] Several studies on the adsorption of peptide molecules on the MoS 2 surface have been reported and indicate that the hydrophobicity, aromatic structure and electrostatic properties of amino acids are important factors affecting adsorption and surface assembly. [87][88][89][90][91][92] However, experimental data remain qualitative in nature, including AFM, TEM imaging, binding information from concentration measurements, QCM, XPS, CD, Raman shis, and relative ranking from washing cycles in phage display. Quantitative binding energies and conformations in solutions are not accessible.…”

“…87 Investigations of the binding of a dodecapeptide (HLLQPTQNPFRN) to MoS 2 suggested signicant binding of Phe and His to MoS 2 , as well as some binding of Arg, and no binding of Leu. 90 These data, however, are at least partly based on simulations and have some uncertainty. Other reported peptides with high binding constants in experiments include GVIHRNDQWTAPGGG and DRWVARDPASIFGGG, as well as a weakly binding/non-binding peptide SVMNTSTKDAIEGGG.…”

Biomarkers and Detection Platforms for Human Health and Performance Monitoring: A Review

“…Also, there is a need to increase the thermal stability and shelf‐life of BREs to extend the operation of wearable devices. To overcome biofunctionalization issues, BREs have been engineered for material binding by the addition of graphene‐ and gold‐binding peptides, [ 90 , 91 , 92 , 93 ] synthesis of thiolated aptamers, and cysteine modified peptides, [ 94 , 95 ] and by the introduction of ligands or cross‐linkable groups for immobilization to sensing material. [ 96 , 97 ] For example, carbon nanotubes were biofunctionalized with an odorant‐binding peptide from honeybees by creating a fusion peptide with a carbon nanotube binding peptide to detect trinitrotoluene.…”

“…Reproduced with permission. [ 92 ] Copyright 2012, IOP Publishing. b) 2‐wire conductance measuring principle for skin conductance.…”

Biofunctionalized Two-dimensional MoS2 Receptors for Rapid Response Modular Electronic SARS-CoV-2 and Influenza A Antigen Sensors

“…2B), which was also examined as a bio-recognition element (BRE) in the current work. The protein was terminated with histidine, reported to bind to MoS2 [26][27] such that its binding domain was expected to possess an orientation toward the sample.…”