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Effect of capping groups at the N- and C-termini on the conformational preference of alpha, beta-peptoids

DOI: 10.1039/c1ob06386c DOI Help

Authors: Emiliana De Santis (Universities of Kent and Greenwich at Medway) , Thomas Hjelmgaard (Clermont Université, Université Blaise Pascal; CNRS) , Cecile Caumes (Clermont Université, Université Blaise Pascal; CNRS) , Sophie Faure (Clermont Université, Université Blaise Pascal; CNRS) , Bruce D. Alexander (University of Greenwich) , Simon J. Holder (University of Kent) , Giuliano Siligardi (Diamond Light Source) , Claude Taillefumier (Clermont Université, Université Blaise Pascal; CNRS) , Alison A. Edwards (Universities of Kent and Greenwich at Medway)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Organic & Biomolecular Chemistry , VOL 10 (5) , PAGES 1108-1122

State: Published (Approved)
Published: November 2011
Diamond Proposal Number(s): 7104

Abstract: Peptoids (N-substituted glycines, i.e. a-peptoids) are artificial oligoamides which are closely related structurally to a-peptides with the side chains located on the amide nitrogen rather than the a-carbon (Fig. 1).1 A major advantage of a-peptoids is their ease of synthesis, particularly by the so-called ‘submonomer method’.2 A further benefit is the vast potential for diversity as the side chains on the amide nitrogens are introduced by primary amines. Therefore a-peptoids are particularly well suited for the construction of peptidomimetic libraries in the context of drug discovery3 as they have been shown to be resistant to proteolytic enzymes.

Journal Keywords: Peptoids; SRCD; B23 Beamline

Subject Areas: Chemistry, Biology and Bio-materials, Medicine


Instruments: B23-Circular Dichroism