Pedro Merino

Bio: Pedro Merino is an academic researcher from University of Zaragoza. The author has contributed to research in topics: Nitrone & Cycloaddition. The author has an hindex of 40, co-authored 370 publications receiving 6216 citations. Previous affiliations of Pedro Merino include University of Ferrara & Technical University of Dortmund.

Catalytic enantioselective hydrophosphonylation of aldehydes and imines

Abstract: In this review, recent advances in catalytic asymmetric hydrophosphonylation of aldehydes and imines are discussed. We also summarize several proposed mechanisms for the different possibilities of asymmetric induction and the application of this catalytic methodology to the enantioselective synthesis of α-amino and α-hydroxy phosphonates. A variety of metal-based chiral catalysts as well as several organic catalysts have been exploited as suitable systems for the preparation of enantiomerically pure phosphonates. The recent evolution and future trends of those and other catalytic systems are described.

Chemical Synthesis of Heterocyclic−Sugar Nucleoside Analogues

Abstract: Dipartimento Farmaco-Chimico, Università di Messina, Via SS Annunziata, 98168 Messina, Italy, Dipartimento di Scienze Chimiche, Università di Catania, Viale Andrea Doria 6, 95125 Catania, Italy, and Laboratorio de Sintesis Asimetrica, Departamento de Quimica Organica, Instituto de Ciencia de Materiales de Aragon, Universidad de Zaragoza, CSIC, E-50009 Zaragoza, Aragon, Spain, Pedro Merino: pmerino@unizar.es

Asymmetric organocatalytic synthesis of γ-nitrocarbonyl compounds through Michael and Domino reactions

Abstract: Recent advances in the organocatalytic enantioselective synthesis of γ-nitrocarbonyl compounds through Michael additions of either nitroalkanes to α,β-unsaturated carbonyl derivatives or enolizable carbonyl compounds to nitroalkenes are surveyed. Domino processes leading to structurally more complex products bearing the γ-nitrocarbonyl functionality are also reviewed.

Organic Reactions in Aqueous Media with a Focus on Carbon−Carbon Bond Formations: A Decade Update

Abstract: 4.2.8. Reductive Coupling 3109 5. Reaction of Aromatic Compounds 3110 5.1. Electrophilic Substitutions 3110 5.2. Radical Substitution 3111 5.3. Oxidative Coupling 3111 5.4. Photochemical Reactions 3111 6. Reaction of Carbonyl Compounds 3111 6.1. Nucleophilic Additions 3111 6.1.1. Allylation 3111 6.1.2. Propargylation 3120 6.1.3. Benzylation 3121 6.1.4. Arylation/Vinylation 3121 6.1.5. Alkynylation 3121 6.1.6. Alkylation 3121 6.1.7. Reformatsky-Type Reaction 3122 6.1.8. Direct Aldol Reaction 3122 6.1.9. Mukaiyama Aldol Reaction 3124 6.1.10. Hydrogen Cyanide Addition 3125 6.2. Pinacol Coupling 3126 6.3. Wittig Reactions 3126 7. Reaction of R,â-Unsaturated Carbonyl Compounds 3127

The ClusPro web server for protein-protein docking.

Abstract: The ClusPro server (https://cluspro.org) is a widely used tool for protein-protein docking. The server provides a simple home page for basic use, requiring only two files in Protein Data Bank (PDB) format. However, ClusPro also offers a number of advanced options to modify the search; these include the removal of unstructured protein regions, application of attraction or repulsion, accounting for pairwise distance restraints, construction of homo-multimers, consideration of small-angle X-ray scattering (SAXS) data, and location of heparin-binding sites. Six different energy functions can be used, depending on the type of protein. Docking with each energy parameter set results in ten models defined by centers of highly populated clusters of low-energy docked structures. This protocol describes the use of the various options, the construction of auxiliary restraints files, the selection of the energy parameters, and the analysis of the results. Although the server is heavily used, runs are generally completed in <4 h.

Asymmetric catalysis by chiral hydrogen-bond donors.

Abstract: Hydrogen bonding is responsible for the structure of much of the world around us. The unusual and complex properties of bulk water, the ability of proteins to fold into stable three-dimensional structures, the fidelity of DNA base pairing, and the binding of ligands to receptors are among the manifestations of this ubiquitous noncovalent interaction. In addition to its primacy as a structural determinant, hydrogen bonding plays a crucial functional role in catalysis. Hydrogen bonding to an electrophile serves to decrease the electron density of this species, activating it toward nucleophilic attack. This principle is employed frequently by Nature's catalysts, enzymes, for the acceleration of a wide range of chemical processes. Recently, organic chemists have begun to appreciate the tremendous potential offered by hydrogen bonding as a mechanism for electrophile activation in small-molecule, synthetic catalyst systems. In particular, chiral hydrogen-bond donors have emerged as a broadly applicable class of catalysts for enantioselective synthesis. This review documents these advances, emphasizing the structural and mechanistic features that contribute to high enantioselectivity in hydrogen-bond-mediated catalytic processes.