Solid-phase peptide synthesis and circular dichroism study of chiral beta-peptoid homooligomers.
N-alkyl-beta-alanine oligomers (beta-peptoids) with alpha-chiral side chains [(R)- or (S)-1-(phenylethyl)amino groups] were synthesized and analyzed by CD spectroscopy. These chiral beta-peptoid homomers exhibited chain-length-dependent and solvent-dependent ellipticity, strongly indicating the presence of a secondary structure in solution. The CD behaviour was only slightly temperature-dependent upon heating, as also previously observed for stable alpha-peptoid helices containing the same type of side chains. Thus, the data presented here comprise the first evidence for a chain length-dependent secondary folding of compounds with this novel peptidomimetic backbone design. In addition, applicability of a novel hyphenated technique, HPLC-SPE-NMR/MS, for analysis of crude SPPS reaction products was demonstrated.
Olsen
C A
CA
Department of Medicinal Chemistry, Faculty of Pharmaceutical Sciences, University of Copenhagen, Copenhagen, Denmark. cao@farma.ku.dk
Lambert
M
M
Witt
M
M
Franzyk
H
H
Jaroszewski
J W
JW
D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D015394:Molecular Structure; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry; D013237:Stereoisomerism
D010455:Peptides