The 3(10)-helix is a relatively common secondary structure motif in peptides and proteins. Its building block is one of various types of beta-bend conformation which comprises an N(alpha)-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 a-helix. Recent applications of rigidified peptide beta-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.

Peptide beta-Bend and 3(10)-Helix: from 3D-Structural Studies to Applications as Templates.

M Crisma;
2005

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 beta-bend conformation which comprises an N(alpha)-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 a-helix. Recent applications of rigidified peptide beta-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.
2005
Istituto di Chimica Biomolecolare - ICB - Sede Pozzuoli
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/164976
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