Related Experiment Video
Updated: Mar 10, 2026
09:22
Self-assembling Morphologies Obtained from Helical Polycarbodiimide Copolymers and Their Triazole Derivatives
Published on: February 7, 2017
8.3K
Self-Assembly, Dynamics, and Polymorphism of hIAPP(20-29) Aggregates at Solid-Liquid Interfaces.
Roozbeh Hajiraissi1, Ignacio Giner1, Guido Grundmeier1
1Technical and Macromolecular Chemistry, Paderborn University , Warburger Strasse 100, 33098 Paderborn, Germany.
Langmuir : the ACS Journal of Surfaces and Colloids
|December 10, 2016
Summary
Surface properties significantly alter amyloid fibril formation and morphology for human islet amyloid polypeptide (hIAPP(20-29)). Hydrophilic surfaces promote diverse fibril types, while hydrophobic surfaces slow aggregation, impacting disease understanding.
Area of Science:
- Biophysics
- Materials Science
- Biochemistry
Background:
- Protein misfolding and amyloid aggregation are central to diseases like type 2 diabetes.
- Environmental factors, particularly interfaces, critically influence protein self-assembly dynamics and aggregate morphology.
- Human islet amyloid polypeptide (hIAPP) aggregation is implicated in type 2 diabetes pathogenesis.
Purpose of the Study:
- To investigate how surfaces with varying physicochemical properties affect the assembly dynamics and aggregate morphology of the amyloidogenic peptide fragment hIAPP(20-29).
- To compare amyloid formation in bulk solution versus on hydrophilic and hydrophobic model surfaces.
Main Methods:
- Time-lapse atomic force microscopy (AFM) was used to observe hIAPP(20-29) assembly.
- Studies were conducted in bulk solution and on hydrophilic (mica) and hydrophobic (hydrocarbon) model surfaces.
Main Results:
- Hydrophilic mica surfaces promoted fibrillation and increased fibril polymorphism compared to bulk solution, yielding straight, coiled, and ribbon-like fibrils.
- Fibrils formed on mica exhibited different dimensions than those in bulk solution.
- Hydrophobic surfaces retarded hIAPP(20-29) fibrillation, unlike previous findings for full-length hIAPP.
- Three distinct fibrillar species were observed on mica, likely forming via protofibril lateral association.
Conclusions:
- Peptide-surface interactions significantly influence amyloid assembly kinetics and fibrillar polymorphism in a peptide-specific manner.
- Understanding these interactions is crucial for elucidating molecular mechanisms of amyloid aggregation at interfaces.
- Findings contribute to insights into the role of surfaces in amyloid-related disease development.
