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Updated: Mar 14, 2026

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
Published on: May 22, 2018
Amyloidogenesis of the amylin analogue pramlintide
Dayana Cabral da Silva1, Giselle N Fontes2, Luiza C S Erthal1
1School of Pharmacy, Federal University of Rio de Janeiro - UFRJ, CCS, Bss24, Ilha do Fundão, 21941-590 Rio de Janeiro, RJ, Brazil.
Abstract:
Amylin is a pancreatic peptide hormone co-secreted along with insulin by the β-cells. It is found in amyloid deposits in both type 2 diabetic individuals and elder non-diabetic. The triple proline amylinomimetic compound (25,28,29-Pro-human amylin) named pramlintide was designed aiming to solve the solubility and amyloid characteristics of human amylin. We have found by using ion mobility spectrometry-based mass spectrometry that pramlintide is able to assembly into multimers. Pramlintide formed amyloid fibrils in vitro in a pH-dependent kinetic process within a few hours, as followed by thioflavin T, quantification of soluble peptide and further characterized by transmission electron microscopy, atomic force microscopy and X-ray diffraction. These data indicate that pramlintide can form amyloid fibers.
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