Electrochemistry represents one of the most intimate ways of interacting with molecules. This review discusses advances in synthetic organic electrochemistry since 2000. Enabling methods and synthetic applications are analyzed alongside innate advantages as well as future challenges of electroorganic chemistry.

Synthetic Organic Electrochemical Methods Since 2000: On the Verge of a Renaissance

The design and implementation of cascade reactions is a challenging facet of organic chemistry, yet one that can impart striking novelty, elegance, and efficiency to synthetic strategies. The application of cascade reactions to natural products synthesis represents a particularly demanding task, but the results can be both stunning and instructive. This Review highlights selected examples of cascade reactions in total synthesis, with particular emphasis on recent applications therein. The examples discussed herein illustrate the power of these processes in the construction of complex molecules and underscore their future potential in chemical synthesis.

Cascade reactions in total synthesis.

The fascinating story of olefin (or alkene) metathesis (eq
1) began almost five decades ago, when Anderson and
Merckling reported the first carbon-carbon double-bond
rearrangement reaction in the titanium-catalyzed polymerization of norbornene. Nine years later, Banks and Bailey reported “a new disproportionation reaction . . . in which olefins are converted to homologues of shorter and longer carbon chains...”. In 1967, Calderon and co-workers named this metal-catalyzed redistribution of carbon-carbon double bonds olefin metathesis, from the Greek word “μeτάθeση”, which means change of position. These contributions have since served as the foundation for an amazing research field, and olefin metathesis currently represents a powerful transformation in chemical synthesis, attracting a vast amount of interest both in industry and academia.

https://core.ac.uk/download/pdf/4884240.pdf

Ruthenium-based heterocyclic carbene-coordinated olefin metathesis catalysts.

Complete Field Guide to Asymmetric BINOL-Phosphate Derived Brønsted Acid and Metal Catalysis: History and Classification by Mode of Activation; Brønsted Acidity, Hydrogen Bonding, Ion Pairing, and Metal Phosphates

Chem. Pharm. Bull.(オピニオン)

/pdf/glyco-ses-selenenylsulfide-mediated-protein-glycoconjugation-10v6fdikg2.pdf

Glyco‐SeS: Selenenylsulfide‐Mediated Protein Glycoconjugation—A New Strategy in Post‐Translational Modification

The endo-β-N-acetylglucosaminidases (ENGases) are an enzyme class (EC 3.2.1.96) produced by a range of organisms, ranging from bacteria, through fungi, to higher order species, including humans, comprising two-sub families of glycosidases which all cleave the chitobiose core of N-linked glycans. Synthetic applications of these enzymes, i.e. to catalyse the reverse of their natural hydrolytic mode of action, allow the attachment of N-glycans to a wide variety of substrates which contain an N-acetylglucosamine (GlcNAc) residue to act as an ‘acceptor’ handle. The use of N-glycan oxazolines, high energy intermediates on the hydrolytic pathway, as activated donors allows their high yielding attachment to almost any amino acid, peptide or protein that contains a GlcNAc residue as an acceptor. The synthetic effectiveness of these biocatalysts has been significantly increased by the production of mutant glycosynthases; enzymes which can still catalyse synthetic processes using oxazolines as donors, but which do not hydrolyse the reaction products. ENGase biocatalysts are now finding burgeoning application for the production of biologically active glycopeptides and glycoproteins, including therapeutic monoclonal antibodies (mAbs) for which the oligosaccharides have been remodelled to optimise effector functions.

/pdf/the-engases-versatile-biocatalysts-for-the-production-of-3pj47vveu7.pdf

The ENGases: versatile biocatalysts for the production of homogeneous N-linked glycopeptides and glycoproteins

Eight pyrrolidine, five pyrrolizidine and one indolizidine analogue(s) of the known alpha-mannosidase inhibitor, the azafuranose, 1,4-dideoxy-1,4-imino-D-mannitol (DIM), have been tested for inhibition of the multiple forms of alpha-mannosidase in human liver in vitro. Substitution of the ring nitrogen markedly decreased or abolished inhibition, but loss of the C-6 hydroxy group, as in 6-deoxy-DIM and 6-deoxy-6-fluoro-DIM, enhanced inhibition, particularly of the lysosomal alpha-mannosidase. Addition of the anomeric substituent-CH2OH decreased inhibition. To be a potent inhibitor of the lysosomal, Golgi II and neutral alpha-mannosidases, a polyhydroxylated pyrrolidine must have the same substituents and chirality as mannofuranose at C-2, C-3, C-4 and C-5. These four chiral centres can also be part of a polyhydroxylated indolizidine, e.g. swainsonine, but not of a pyrrolizidine, e.g. cyclized DIM, ring-contracted swainsonine or 1,7-diepi-australine. DIM did not inhibit lysosomal alpha-mannosidase intracellularly, but both 6-deoxy-DIM and 6-deoxy-6-fluoro-DIM caused accumulation of partially catabolized glycans in normal human fibroblasts. Analysis of these induced storage products by h.p.l.c. showed that both compounds also inhibited Golgi alpha-mannosidase II and that 6-deoxy-6-fluoro-DIM was also a good inhibitor of the endoplasmic reticulum alpha-mannosidase and specific lysosomal alpha (1-6)-mannosidase. None of the mannofuranose analogues appeared to inhibit Golgi alpha-mannosidase I.

/pdf/the-structural-basis-of-the-inhibition-of-human-alpha-361ypjkja5.pdf

The structural basis of the inhibition of human alpha-mannosidases by azafuranose analogues of mannose.

Glycosylation catalyzed by a chiral Brønsted acid.

Dairy products are heated both during processing and by consumers during food preparation; consumers place a high level of importance on flavour when assessing product acceptability. Of particular importance to the flavour of heated dairy products is the highly complex network of Maillard reactions. Much focus has been placed on the undesirable flavours generated through the Maillard reaction and how to minimise the formation of these flavours. However, beneficial flavours can also be formed by the Maillard reaction; dairy products, such as ghee, are formed by heating and are characterised by the unique flavour generated by this chemistry. This review looks at the Maillard reaction as a source of beneficial flavours for cooked dairy products and the application of models to the study of flavour formation in food systems. Models are typically used to study complex reactions in a simplified way; however, they are not always applicable to food systems.

The role of the Maillard reaction in the formation of flavour compounds in dairy products – not only a deleterious reaction but also a rich source of flavour compounds

Antony J. Fairbanks

Papers

Glyco‐SeS: Selenenylsulfide‐Mediated Protein Glycoconjugation—A New Strategy in Post‐Translational Modification

The ENGases: versatile biocatalysts for the production of homogeneous N-linked glycopeptides and glycoproteins

The structural basis of the inhibition of human alpha-mannosidases by azafuranose analogues of mannose.

Glycosylation catalyzed by a chiral Brønsted acid.

The role of the Maillard reaction in the formation of flavour compounds in dairy products – not only a deleterious reaction but also a rich source of flavour compounds