Owing to high resolution, reliability, and industrial compatibility, all-photolithography is a promising strategy for industrial manufacture of organic electronics. However, it receives limited success due to the absence of a semiconducting photoresist with high patterning resolution, mobility, and performance stability against photolithography solution processes. Here, we develop a comprehensive semiconducting photoresist with nano-interpenetrating structure. After photolithography, nanostructured cross-linking networks interpenetrate with continuous phases of semiconducting polymers, enabling submicrometer patterning accuracy and compact molecular stacking with high thermodynamic stability. The mobility reaches the highest values of photocrosslinkable organic semiconductors and maintains almost 100% after soaking in developer and stripper for 1000 min. Owing to the comprehensive performance, all-photolithography is achieved, which fabricates organic inverters and high-density transistor arrays with densities up to 1.1 × 10⁵ units cm⁻² and 1 to 4 orders larger than conventional printing processes, opening up a new approach toward manufacturing highly integrated organic circuits and systems.

Quantifying interactions between biomolecules subject to various environmental conditions is essential for applications such as drug discovery and precision medicine. This paper presents an investigation of the kinetics of environmentally dependent biomolecular binding using an electrolyte-gated graphene field-effect transistor (GFET) nanosensor. In this approach, biomolecular binding occurring on and in the vicinity of a graphene surface induces a change in carrier concentration, whose resulting conductance change is measured. This allows a systematic study of the kinetic properties of the binding system. We apply this approach to the specific binding of human immunoglobulin E (IgE), an antibody involved in parasite immunity, with an aptamer at different ionic strengths (Na⁺ and Mg²⁺) and temperatures. Experimental results demonstrate increased-rate binding kinetics at higher salt-ion concentrations and temperatures. In particular, the divalent cation Mg²⁺ yields more pronounced changes in the conformational structure of the aptamer than the monovalent cation Na⁺. In addition, the dissociation of the aptamer-protein complex at room temperature is found to be characterized by large unfavorable changes in the activation enthalpy and entropy.