Effect of a cis-4-Aminopiperidine-3-carboxylic Acid (cis-APiC) Residue on Mixed-helical Folding of Unnatural Peptides

The α/β-peptide 11/9-helix and the β-peptide 12/10-helix belong to “mixed” helices, in which two types of hydrogen bonds with opposite directionality alternate along the helical axis. cis-2-Aminocyclohaxanecarboxylic acid (cis-ACHC) is...

The agent for increasing soybean yield and for the Round-up resistant one decrease in the synthesis of unnatural peptides with glycine glyphosate

The purpose. In order to increase soybean yield to develop the agent for pre-sowing seed treatment and crop spraying in the budding phase, and application of an agent for Round-up resistant soybean should reduce the synthesis of unnatural peptides with glycine glyphosate in the structure of proteins, which can cause unpredictable consequences for animals and humans. Methods. Laboratory and field experiments on chickens and hens. Results. The agent «Zernovit» for pre-sowing seed treatment of soybean seeds (patent of Ukraine for utility model No.119739, 2017) and in the budding phase has been developed. In addition, the formation of unnatural peptides of glycine glyphosate in the structure of proteins decreases through the stimulation of protein synthesis in the genetically modified soybean when applying «Zernovit». Conclusions. The agent «Zernovit» for pre-sowing soybean seed treatment and application in the budding phase, which provides an increase by 16.8 % in yields against the control of 2.8 t/ha, has been developed and tested in the conditions of production, and when it is used in genetically modified soybean it reduces the synthesis of unnatural peptides with glycine glyphosate in the structure of soybean protein when sprayed with Round-up. This is due to the stimulation of the protein synthesis that prevents the inclusion of glycine glyphosate in the unnatural peptides of the protein synthesis.

Co-assembly of helical β3-peptides: a self-assembled analogue of a statistical copolymer

Unnatural peptide self-assembly offers the means to design hierarchical nanostructures of controlled geometries, chemical function and physical properties. N-acyl β3 peptides, where all residues are unnatural amino acids, are able to form helical fibrous structures by a head-to-tail assembly of helical monomers, extending the helix via a three point supramolecular hydrogen bonding motif. These helical nanorods were shown to be stable under a wide range of physical conditions, offering a self-assembled analogue of polymeric fibres. Hitherto the self-assembly has only been demonstrated between identical monomers; however the self-assembly motif is sequence-independent, offering the possibility of hetero-assembly of different peptide monomers. Here we present a proof of principle study of head-to-tail co-assembly of two different helical unnatural peptides Ac-β3[WELWEL] and Ac-β3[LIA], where the letters denote the β3 analogues of natural amino acids. By atomic force microscopy imaging it was demonstrated that the homo-assembly and co-assembly of these peptides yield characteristically different structures. Synchrotron small angle X-ray scattering experiments have confirmed the presence of the fibres in the solution and the averaged diameters from modelled data correlate well to the results of AFM imaging. Hence, there is evidence of co-assembly of the fibrous superstructures; given that different monomers may be used to introduce variations into chemical and physical properties, the results demonstrate a self-assembled analogue of a statistical co-polymer that can be used in designing complex functional nanomaterials.