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pH-controlled aggregation polymorphism of amyloidogenic Aβ(16-22): insights for obtaining peptide tapes and peptide nanotubes, as function of the N-terminal capping moiety.

Autor: Elgersma RC; Medicinal Chemistry and Chemical Biology, Utrecht Institute for Pharmaceutical Sciences, Department of Pharmaceutical Sciences, Faculty of Science, Utrecht University, P.O. Box 80082, 3508 TB Utrecht, The Netherlands., Kroon-Batenburg LM; Division of Crystal and Structural Chemistry, Bijvoet Center for Biomolecular Research, Department of Chemistry, Faculty of Science, Utrecht University, 3584 CH Utrecht, The Netherlands., Posthuma G; Department of Cell Biology, Center for Electron Microscopy, University Medical Center, 3508 GA Utrecht, The Netherlands., Meeldijk JD; Division of Inorganic Chemistry and Catalysis, Department of Chemistry, Faculty of Science, Utrecht University, 3508 TB Utrecht, The Netherlands., Rijkers DT; Medicinal Chemistry and Chemical Biology, Utrecht Institute for Pharmaceutical Sciences, Department of Pharmaceutical Sciences, Faculty of Science, Utrecht University, P.O. Box 80082, 3508 TB Utrecht, The Netherlands. Electronic address: D.T.S.Rijkers@uu.nl., Liskamp RM; Medicinal Chemistry and Chemical Biology, Utrecht Institute for Pharmaceutical Sciences, Department of Pharmaceutical Sciences, Faculty of Science, Utrecht University, P.O. Box 80082, 3508 TB Utrecht, The Netherlands; Chemical Biology and Medicinal Chemistry, School of Chemistry, University of Glasgow, Joseph Black Building, University Avenue, Glasgow G12 8QQ, United Kingdom. Electronic address: R.M.J.Liskamp@uu.nl.

Publikováno v: European journal of medicinal chemistry [Eur J Med Chem] 2014 Dec 17; Vol. 88, pp. 55-65. Date of Electronic Publication: 2014 Jul 25.

pH controlled aggregation morphology of Abeta(16-22): formation of peptide nanotubes, helical tapes and amyloid fibrils.

Autor: Elgersma RC; Medicinal Chemistry & Chemical Biology, Utrecht Institute for Pharmaceutical Sciences, Department of Pharmaceutical Sciences, Faculty of Science, Utrecht University, Utrecht, The Netherlands., Rijkers DT, Liskamp RM

Publikováno v: Advances in experimental medicine and biology [Adv Exp Med Biol] 2009; Vol. 611, pp. 239-40.

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

Autor: Elgersma RC; Department of Medicinal Chemistry and Chemical Biology, Utrecht Institute for Pharmaceutical Sciences, The Netherlands., Posthuma G, Rijkers DT, Liskamp RM

Publikováno v: Journal of peptide science : an official publication of the European Peptide Society [J Pept Sci] 2007 Nov; Vol. 13 (11), pp. 709-16.

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

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

Publikováno v: Organic & biomolecular chemistry [Org Biomol Chem] 2006 Oct 07; Vol. 4 (19), pp. 3587-97. Date of Electronic Publication: 2006 Aug 21.