Organic Syntheses vs Dimer dice

OrgSyn app brings all published procedures right to your fingertips. Search for full volume or single article or use full text search to find exactly what you are looking for. Share your findings with colleagues. Save hitlists and procedures to view them later, even offline. Since 1921, Organic Syntheses has provided the chemistry community with detailed, reliable, and carefully checked procedures for the synthesis of organic compounds. Some procedures describe practical methods for the preparation of specific compounds of interest, while other procedures illustrate important synthetic methods with general utility. Each procedure is written in considerably more detail as compared to typical experimental procedures in other journals, and each reaction with its characterization data has been repeated several times and carefully "checked" for reproducibility in the laboratory of a member of the Board of Editors. Organic Syntheses is published by Organic Syntheses, Inc., a non-profit corporation. Online Edition ISSN 2333-3553 Print Edition ISSN 0078-6209

DimerDice allows visualizing different supramolecular dimeric complexes of cyclic peptides in Augmented Reality (AR). The cyclic peptides (CPs) are composed by γ-amino acids (cis-α,γ-aminocycloalkanecarboxylic acids, γ-Acas) alternated with α-amino acids (α,γ-CPs). These peptides containing γ-Acas can be designed from the original D,L-α-CPs just by replacing any α-amino acid for a γ-Aca of equivalent chirality. For instance, L-amino acids can be replaced by (1R,3S)-isomers while the (1S,3R)-Acas would substitute the D-enantiomers. As part of an in-vitro/in-silico study carried out at Santiago de Compostela University to deeply analyze the preferred rearrangement adopted by α,γ-CPs, we explored all the possible combinations that could take place starting from two different monomers and their corresponding enantiomers.[1] This approach uses the selective N-methylation of the amide groups whose protons are not involved in hydrogen bonding interactions. The N-methylated residues are indicated in the figures of the trackers. Depending on the combination of monomers, a parallel or an antiparallel arrangement is possible. Pointing with the device to each tracker separately, an AR image of the corresponding monomer is viewed. When the tracker images of two monomers are placed close to each other, the structure of the dimer formed by that combination of cyclic peptides is shown. Full geometry optimizations of the dimers and monomers were carried out with the B3LYP functional and the standard 6-31G(d) basis set. All of the DFT calculations reported in this study were performed with the Gaussian 16 package. This application was specifically developed by Santiago de Compostela University (Spain) and MD.USE Innovative Solutions S.L. (www.mduse.com). [1] Manuscript in preparation.