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Biomolecule-based piezoelectric nanostructures emerged as a new class of energy-converse materials, and designing tailored piezoelectric amino acid arrays is essential to achieve efficient electrical-mechanical coupling and fulfill their application potential. However, the controlled growth of amino acid nanostructures is still challenging due to the limited understanding of their growth mechanism. Herein, we base on the Stranski-Krastanov (S-K) growth mode and propose a mechanism for the growth of ordered amino acid array structures via physical vapor deposition. The growth of vertical valine sheet arrays is examined by changing the substrate temperature, chamber pressure, and source-substrate distance, and a "layer-plus-sheet" growth process is revealed. The modified S-K growth mode is applied to fabricate other amino acid nanostructures like leucine and isoleucine. The growth mode not only explains the formation of uniform and controllable morphology of amino acid structures but also leads to the significant enhancement of their piezoelectric properties. The maximal effective piezoelectric constant of valine sheets is 11.4 pm V -1 , which approaches its highest predicted value. The output voltage of the valine array-based nanogenerator is ∼4.6 times the output voltage of the valine powder-based nanogenerator. This work provides new insights into the growth mechanism of ordered piezoelectric amino acid arrays, making them promising candidates for applications in wearable or implantable electronic devices.

Site-specific incorporation of non-canonical amino acids (ncAAs) into proteins has emerged as a universal tool for systems bioengineering at the interface of chemistry, biology, and technology. The diversification of the repertoire of the genetic code has been achieved for amino acids with long and/or bulky side chains equipped with various bioorthogonal tags and useful spectral probes. Although ncAAs with relatively small side chains and similar properties are of great interest to biophysics, cell biology, and biomaterial science, they can rarely be incorporated into proteins. To address this gap, we report the engineering of PylRS variants capable of incorporating an entire library of aliphatic "small-tag" ncAAs. In particular, we performed mutational studies of a specific PylRS, designed to incorporate the shortest non-bulky ncAA ( S -allyl-l-cysteine) possible to date and based on this knowledge incorporated aliphatic ncAA derivatives. In this way, we have not only increased the number of translationally active "small-tag" ncAAs, but also determined key residues responsible for maintaining orthogonality, while engineering the PylRS for these interesting substrates. Based on the known plasticity of PylRS toward different substrates, our approach further expands the reassignment capacities of this enzyme toward aliphatic amino acids with smaller side chains endowed with valuable functionalities.

The title compound, C 6 H 11 NO 2 ·2H 2 O 2 , is the richest (by molar ratio) in hydrogen peroxide among the peroxosolvates of aliphatic α-amino acids. The asymmetric unit contains a zwitterionic pipecolinic acid mol-ecule and two hydrogen peroxide mol-ecules. The two crystallographically independent hydrogen peroxide mol-ecules form a different number of hydrogen bonds: one forms two as donor and two as acceptor ([2,2] mode) and the other forms two as donor and one as acceptor ([2,1] mode). The latter hydrogen peroxide mol-ecule forms infinite hydrogen-bonded hydro-peroxo chains running along the c -axis direction, which is unusual for aliphatic α-amino acid peroxosolvates., (© Navasardyan et al. 2020.)

Background: Amino acids are the essential building blocks of proteins and, therefore, living organisms. While the focus often lies on the canonical or proteinogenic amino acids, there is also a large number of non-canonical amino acids to explore. Some of them are part of toxins or antibiotics in fungi, bacteria or animals (e.g. sponges). Some others operate at the translational level like an "undercover agent"., Scope of Review: Here we give an overview of natural aliphatic amino acids, up to a side chain length of five carbons, without rings and with an unmodified backbone, and have a closer look on each of them. Some of them are dehydro amino acids with double or even triple bonds. Moreover, we outline mathematical methods for enumerating the complete list of all potential aliphatic amino acids of a given chain length. This should be of interest for synthetic biology., Major Conclusions: Most non-proteinogenic amino acids are found within fungi, with particularly many produced by Amanita species as defence chemicals. Several are incorporated into peptide antibiotics. Some of the amino acids occur due to broad substrate specificity of the branched-chain amino acid synthesis pathways. A large variety of amino acids were also found in the Murchison meteorite., General Significance: Non-proteinogenic amino acids are of interest for numerous medical applications: discovery of new antibiotics, support in designing synthetic antibiotics, improvement of protein and peptide pharmaceuticals by avoiding incorporation of non-canonical amino acids, study of toxic cyanobacteria and other applications., (Copyright © 2016 Elsevier B.V. All rights reserved.)