Backbone-modified amylin derivatives: implications for amyloid inhibitor design and as template for self-assembling bionanomaterials

Elgersma, R.C., Posthuma, G., Rijkers, D.T.S. and Liskamp, R.M.J. (2007) Backbone-modified amylin derivatives: implications for amyloid inhibitor design and as template for self-assembling bionanomaterials. Journal of Peptide Science, 13(11), pp. 709-716. (doi:10.1002/psc.831)

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Abstract

This report reviews our approach to the design, synthesis and structural/morphological analysis of backbone-modified amylin(20–29) derivatives. Depending on the position in the peptide backbone and the type of amide bond isostere/modification, the amylin(20–29) peptides behave either as inhibitors of amyloid fibril formation, which are able to retard amyloid formation of native amylin(20–29), or as templates for the formation of self-assembled supramolecular structures. Molecular fine-tuning of the hydrogen-bond accepting/donating properties allows the control over the morphology of the supramolecular aggregation motifs such as helical ribbons and tapes, ribbons progressing to closed peptide nanotubes, (twisted) lamellar sheets or amyloid fibrils.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Liskamp, Professor Robert
Authors: Elgersma, R.C., Posthuma, G., Rijkers, D.T.S., and Liskamp, R.M.J.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Journal of Peptide Science
Publisher:John Wiley & Sons Ltd.
ISSN:1075-2617
ISSN (Online):1099-1387

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