Peptide β-Bend and 3
10
-Helix: from 3D-Structural Studies to Applications as Templates |
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| Authors: | Claudio Toniolo Marco Crisma Fernando Formaggio Cristina Peggion Quirinus Broxterman Bernard Kaptein |
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| Institution: | (1) Institute of Biomolecular Chemistry, CNR, Department of Chemistry, University of Padova, 35131 Padova, Italy;(2) DSM Pharma Chemicals, Advanced Synthesis and Catalysis, P.O. Box 18, 6160, MD, Geleen, The Netherlands |
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| Abstract: | The 3 10-helix is a relatively common secondary structure motif in peptides and proteins. Its building block is one of various types of β-bend conformation which comprises an N α-acylated dipeptide alkylamide system. A complete 3D-structural characterization of this ternary helix has been achieved, thus allowing its unambiguous discrimination from the closely related α-helix. Recent applications of rigidified peptide β-bends and 3 10-helices as templates for investigations in synthetic organic chemistry (macrocyclization, catalysis), host–guest chemistry (molecular recognition), and physical chemistry (donor–acceptor interaction) will be discussed. |
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| Keywords: | β -bend catalysis donor– acceptor interaction 3 10-helix host– guest chemistry macrocyclization peptide conformation Cα -tetrasubstituted α -amino acids |
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