| Autor: |
Elgersma RC; Department of Medicinal Chemistry and Chemical Biology, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, PO Box 80082, 3508 TB, Utrecht, The Netherlands., Meijneke T, de Jong R, Brouwer AJ, Posthuma G, Rijkers DT, Liskamp RM |
| Jazyk: |
angličtina |
| Zdroj: |
Organic & biomolecular chemistry [Org Biomol Chem] 2006 Oct 07; Vol. 4 (19), pp. 3587-97. Date of Electronic Publication: 2006 Aug 21. |
| DOI: |
10.1039/b606875h |
| Abstrakt: |
The incorporation of a single beta-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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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