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Modern Supramolecular Chemistry: Strategies for Macrocycle by Francois Diederich, Peter Stang, Rik R. Tykwinski

By Francois Diederich, Peter Stang, Rik R. Tykwinski

Written through the world over acclaimed specialists, this useful quantity covers all significant periods of supramolecular compounds. Chapters contain cyclophanes, resorcinarene and calixarene synthesis, supramolecular metallomacrocycles and macrocycle synthesis, rotaxane and catenane synthesis, cucurbiturils and porphyrins, in addition to macrocyclic drugs.Each bankruptcy includes experimental methods permitting quick entry to this kind of man made chemistry.

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When catalyst F1 is employed, whose activity is comparable to that of first-generation Grubbs catalyst G1, the E-isomer is obtained as the major product. The E/Z ratio does not evolve with time, proving that the reaction is under kinetic control with this catalyst. Herbarumin II precursor E-35 (R¼OMOM) is also synthesized with an excellent selectivity using F1. A similar observation was made by Marco and coworkers when synthesizing microcarpalide [29]. 14). These compounds could be separated by chromatography and the E-isomer was subsequently converted to microcarpalide by removal of the MOM and the acetonide protecting groups.

2002) Proc. Natl. Acad. Sci. , 99, 12037–12042. For a review on sponge peptides: Fusetani, N. and Matsunaga, S. (1993) Chem. , 93, 1793–1806. Since the original paper by Fusetani and Matsunaga [39], Hagihara and Schreiber reassigned the stereochemistry of the vinylogous tyrosine- and a-ketoarginine residue to be of the S-configuration Hagihara, M. L. (1992) J. Am. Chem. , 114, 6570–6571. R. , Nicolaou, K. H. and Fusetani, N. (1993) Proc. Natl. Acad. Sci. L. and Clardy, J. (1993) J. Am. Chem. , Lee, A.

Org)]. 15 Structures of synthetic Grb2 SH2 domain-binding analogs [58—60]. 3 Selected Cyclic Peptides The recognition of phosphorylated peptides by SH2 domains depends on the phosphorylated residue. Specificity is determined by one or two nearby residues. Apart from the phosphotyrosine-specific recognition, SH2-domains can interact in different ways with other proteins [55]. This paragraph focuses on the interactions mediated by the conventional phosphopeptide recognition region. ) Although most SH2 domains bind their phosphorylated peptide ligands in an extended, b-strandlike conformation, the Grb2 SH2 domain binds the natural ligand in a type I bturn conformation [58].

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