The self‐assembly of biomolecules can provide a new approach for the design of functional systems with a diverse range of hierarchical nanoarchitectures and atomically defined structures. In this regard, peptides, particularly short peptides, are attractive building blocks because of their ease of establishing structure–property relationships, their productive synthesis, and the possibility of their hybridization with other motifs. Several assembling peptides, such as ionic‐complementary peptides, cyclic peptides, peptide amphiphiles, the Fmoc‐peptide, and aromatic dipeptides, are widely studied. Recently, studies on material synthesis and the application of tyrosine‐rich short peptide‐based systems have demonstrated that tyrosine units serve as not only excellent assembly motifs but also multifunctional templates. Tyrosine has a phenolic functional group that contributes to π–π interactions for conformation control and efficient charge transport by proton‐coupled electron‐transfer reactions in natural systems. Here, the critical roles of the tyrosine motif with respect to its electrochemical, chemical, and structural properties are discussed and recent discoveries and advances made in tyrosine‐rich short peptide systems from self‐assembled structures to peptide/inorganic hybrid materials are highlighted. A brief account of the opportunities in design optimization and the applications of tyrosine peptide‐based biomimetic materials is included.
A novel platform is proposed to quantify the coupling phenomenon between electrons and protons in tyrosine-rich peptide/manganese oxide hybrid films at room temperature.
Transient electronics is a good platform for human implantable biomedical devices for diagnosing diseases and delivering therapeutic materials because additional surgery is not required to retrieve the device. Surrounding bio‐fluids inevitably dissolve device components, and the remaining electronic debris can trigger hazardous inflammation reactions within human body. Therefore, it is important to reduce the total dissolution time of devices even after they stop working. Thus, fast‐dissolving tyrosine‐based peptides are suggested as an insulator instead of SiO2, which has been used as a dissolution retarder in transient electronics. By combining a peptide insulator, zinc oxide semiconductor, and tungsten conductor, a biocompatible and biodegradable thin film transistor is fabricated. The device exhibits moderate performance (ON/OFF >103 and field‐effect mobility of ≈0.6 cm2 V−1 s−1) and is fast‐dissolving (<3 h) in bio‐fluids.
Here, we explore the possibility of using peptide-based materials as a membrane in solid-state nanopore devices in an effort to develop a sequence-specific, programmable biological membrane platform. We use a recently developed tyrosine-mediated self-assembly peptide sheet. At the air/water interface, the 5mer peptide YFCFY self-assembles into a uniform and robust two-dimensional (2D) structure, and the peptide sheet is easily transferred to a low-noise glass substrate. The thickness of the peptide membrane can be adjusted to approximately 5 nm (or even to 2 nm) by an etching process, and the diameters of the peptide nanopores can be precisely controlled using a focused electron beam with an attuned spot size. The ionic current noise of the peptide nanopore is comparable to those of typical silicon nitride nanopores or multilayer 2D materials. Using this membrane, we successfully observe translocation of 1000 bp double-stranded DNA with a sufficient signal-to-noise ratio of ∼30 and an elongated translocation speed of ∼1 bp μs−1. Our results suggest that the self-assembled peptide film can be used as a sensitive nanopore membrane and employed as a platform for applying biological functionalities to solid-state substrates.
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