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

Elgersma, R.C., Meijneke, T., de Jong, R., Brouwer, A.J., Posthuma, G., Rijkers, D.T.S. and Liskamp, R.M.J. (2006) Synthesis and structural investigations of N-alkylated ?-peptidosulfonamide?peptide hybrids of the amyloidogenic amylin(20?29) sequence: implications of supramolecular folding for the design of peptide-based bionanomaterials. Organic and Biomolecular Chemistry, 4, pp. 3587-3597. (doi:10.1039/b606875h)

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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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Liskamp, Professor Robert
Authors: Elgersma, R.C., Meijneke, T., de Jong, R., Brouwer, A.J., Posthuma, G., Rijkers, D.T.S., and Liskamp, R.M.J.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Organic and Biomolecular Chemistry
Publisher:Royal Society of Chemistry
ISSN:1477-0520

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