Automated solid-phase synthesis and structural investigation of -peptidosulfonamides and -peptidosulfonamide/-peptide hybrids: -peptidosulfonamide and -peptide foldamers are two of a different kind

de Jong, R., Rijkers, D.T.S. and Liskamp, R.M.J. (2002) Automated solid-phase synthesis and structural investigation of -peptidosulfonamides and -peptidosulfonamide/-peptide hybrids: -peptidosulfonamide and -peptide foldamers are two of a different kind. Helvetica Chimica Acta, 85(12), pp. 4230-4243. (doi: 10.1002/hlca.200290008)

Abstract

Fmoc-protected β-aminoethane sulfonylchlorides can be employed for efficient automated solid phase synthesis of β-peptidosulfonamides and β-peptidosulfonamide/β-peptide hybrids containing one or more β-peptidosulfonamide residues. Thus, Fmoc-protected β-aminoethane sulfonylchlorides 5a–c led to the hexa-β-peptidosulfonamide 9 and the nona-β-peptidosulfonamide 10. In addition, the β-peptidosulfonamide/β-peptide hybrids 13 and 16, consisting of six and nine β-residues, respectively, and containing a single β-peptidosulfonamide unit in the middle, as well as the peptidosulfonamide/β-peptide hybrid 15 with nine β-residues, including an N-terminal β-peptidosulfonamide residue, were synthesized by automated solid-phase synthesis. Both CD and NMR spectroscopic measurements did not indicate any helical secondary structure for 9 and 10. As was shown by CD-measurements, the β-peptidosulfonamide residue in the hybrids 13, 15, and 16 acts as a ‘helix breaker', especially when located in the middle of the hybrid chain (13 and 16), but, although to a lesser extent, also at the N-terminus.

• Item Type: Articles
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Liskamp, Professor Robert
• Authors: de Jong, R., Rijkers, D.T.S., and Liskamp, R.M.J.
• College/School: College of Science and Engineering > School of Chemistry
• Journal Name: Helvetica Chimica Acta
• ISSN: 0018-019X
• ISSN (Online): 1522-2675