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Conventional chemical approaches for synthesizing nanoparticles (NPs) may restrict their applicability as they are not eco-friendly, energetically efficient and often involve toxic reducing/capping agents; but phytonanotechnology enabled the synthesis of safe, inexpensive, highly biocompatible NPs. In this regard, thorough understanding of green components and the modulatory effects of different reaction conditions on the physicochemical parameters of green synthesized NPs would be a prerequisite, which is not depicted elsewhere. This review critically analyzes the relevant reaction conditions from their mechanistic viewpoints in plant-based synthesis of NPs arising fundamental issues which need to be determined carefully. The size, stability and surface chemistry of phytogenic NPs may be fabricated as a function of multiple interconnected reaction parameters and the plant species used. The therapeutic potential of phytogenic NPs may depend on the plant species used; and so the meticulous understanding of physicochemical parameters and the family wise shorting of elite plant species may potentially benefit the theranostic future of plant-based NPs.

The HisJ protein from Escherichia coli and related Gram negative bacteria is the periplasmic component of a bacterial ATP-cassette (ABC) transporter system. Together these proteins form a transmembrane complex that can take up L-histidine from the environment and translocate it into the cytosol. We have studied the specificity of HisJ for binding L-His and many related naturally occurring compounds. Our data confirm that L-His is the preferred ligand, but that 1-methyl-L-His and 3-methyl-L-His can also bind, while the dipeptide carnosine binds weakly and D-histidine and the histidine degradation products, histamine, urocanic acid and imidazole do not bind. L-Arg, homo-L-Arg, and post-translationally modified methylated Arg-analogs also bind with reasonable avidity, with the exception of symmetric dimethylated-L-Arg. In contrast, L-Lys and L-Orn have considerably weaker interactions with HisJ and methylated and acetylated Lys variants show relatively poor binding. It was also observed that the carboxylate group of these amino acids and their variants was very important for proper recognition of the ligand. Taken together our results are a key step towards designing HisJ as a specific protein-based reagentless biosensor.