Über Lie-Ringe von Gruppen und ihre universellen Enveloppen

Ohne Zusammenfassung     

Replacement of Water Molecules in a Phosphate Binding Site by Furanoside‐Appended lin‐Benzoguanine Ligands of tRNA‐Guanine Transglycosylase (TGT)

The enzyme tRNA‐guanine transglycosylase has been identified as a drug target for the foodborne illness shigellosis. A key challenge in structure‐based design for this enzyme is the filling of the polar ribose‐34 pocket. Herein, we describe a novel series of ligands consisting of furanoside‐appended lin‐benzoguanines. They were designed to replace a conserved water cluster and differ by the functional groups at C(2) and C(3) of the furanosyl moiety being either OH or OMe. The unfavorable desolvation of Asp102 and Asp280, which are located close to the ribose‐34 pocket, had a significant impact on binding affinity. While the enzyme has tRNA as its natural substrate, X‐ray co‐crystal structures revealed that the furanosyl moieties of the ligands are not accommodated in the tRNA ribose‐34 site, but at the location of the adjacent phosphate group. A remarkable similarity of the position of the oxygen atoms in these two structures suggests furanosides as a potential phosphate isoster.     

On the number of types of finite dimensional Hopf algebras

For an odd prime p we construct an infinite class of non-isomorphic Hopf algebras of dimension p ⁴ over an infinite field containing primitive p-th roots of unity, answering in the negative a long standing conjecture of Kaplansky. Oblatum 6-XI-1997 / Published online: 12 November 1998     

On pointed Hopf algebras of dimension

In this note we describe nonsemisimple Hopf algebras of dimension with coradical isomorphic to , abelian of order , over an algebraically closed field of characteristic zero. If is cyclic or , then we also determine the number of isomorphism classes of such Hopf algebras.

     

Peptide-Catalyzed Stereoselective Conjugate Addition Reaction of Aldehydes to C-Substituted Maleimides

Catalytic stereoselective additions with maleimides are useful one-step reactions to yield chiral succinimides, molecules that are widespread among therapeutically active compounds but challenging to prepare when the maleimide is C-substituted. We present the tripeptide H-Pro-Pro-Asp-NHC₁₂H₂₅ as a catalyst for conjugate addition reactions between aldehydes and C-substituted maleimides to form succinimides with three contiguous stereogenic centers in high yields and stereoselectivities. The peptidic catalyst is so chemoselective that no protecting group is needed at the imide nitrogen of the maleimides. Derivatization of the succinimides was straightforward and provided access to chiral pyrrolidines, lactones, and lactams. Kinetic studies, including a Hammett plot, provided detailed insight into the reaction mechanism.     

Peptide‐Catalyzed Stereoselective Conjugate Addition Reactions of Aldehydes to Maleimide

The tripeptide H‐d Pro‐Pro‐Asn‐NH₂ is presented as a catalyst for asymmetric conjugate addition reactions of aldehydes to maleimide. The peptidic catalyst promotes the reaction between various aldehydes and unprotected maleimide with high stereoselectivities and yields. The obtained products were readily derivatized to the corresponding pyrrolidines, lactams, lactones, and peptide‐like compounds. ¹H NMR spectroscopic, crystallographic, and computational investigations provided insight into the conformational properties of H‐d Pro‐Pro‐Asn‐NH₂ and revealed the importance of hydrogen bonding between the peptide and maleimide for catalyzing the stereoselective C?C bond formation.