Issue 19, 2006

Synthesis and structural investigations of N-alkylated β-peptidosulfonamide–peptide hybrids of the amyloidogenic amylin(20–29) sequence: implications of supramolecular folding for the design of peptide-based bionanomaterials

Abstract

The incorporation of a single β-aminoethane sulfonyl amide moiety in a highly amyloidogenic peptide sequence resulted in a complete loss of amyloid fibril formation. Instead, supramolecular folding morphologies were observed. Subsequent chemoselective N-alkylation of the sulfonamide resulted in amphiphilic peptide-based hydrogelators. It was found that variation of merely the alkyl chain induced a dramatic variation in aggregation motifs such as helical ribbons and tapes, ribbons progressing to closed tubes, twisted lamellar sheets and entangled/branched fibers.

Graphical abstract: Synthesis and structural investigations of N-alkylated β-peptidosulfonamide–peptide hybrids of the amyloidogenic amylin(20–29) sequence: implications of supramolecular folding for the design of peptide-based bionanomaterials

Article information

Article type
Paper
Submitted
15 May 2006
Accepted
27 Jul 2006
First published
21 Aug 2006

Org. Biomol. Chem., 2006,4, 3587-3597

Synthesis and structural investigations of N-alkylated β-peptidosulfonamide–peptide hybrids of the amyloidogenic amylin(20–29) sequence: implications of supramolecular folding for the design of peptide-based bionanomaterials

R. C. Elgersma, T. Meijneke, R. de Jong, A. J. Brouwer, G. Posthuma, D. T. S. Rijkers and R. M. J. Liskamp, Org. Biomol. Chem., 2006, 4, 3587 DOI: 10.1039/B606875H

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