Bridging the gap between the nanostructural organization and macroscopic interfacial rheology of amyloid fibrils at liquid interfaces
The interfacial behavior of proteins and protein aggregates such as fibrils influences the bulk behavior of multiphase systems in foods, pharmaceuticals, and other technological applications. Additionally, it is an important factor in some biological processes such as the accumulation of amyloid fib...
Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 30(2014), 33 vom: 26. Aug., Seite 10090-7 |
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Weitere Verfasser: | , , , , |
Format: | Online-Aufsatz |
Sprache: | English |
Veröffentlicht: |
2014
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Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Amyloid Lactoglobulins |
Zusammenfassung: | The interfacial behavior of proteins and protein aggregates such as fibrils influences the bulk behavior of multiphase systems in foods, pharmaceuticals, and other technological applications. Additionally, it is an important factor in some biological processes such as the accumulation of amyloid fibrils at biological membranes in neurodegenerative diseases. Here, using β-lactoglobulin fibrils as a model system, we cover a large range of characteristic measuring length scales by combining atomic force microscopy, passive probe particle tracking, tensiometry, interfacial shear, and dilatational rheology in order to correlate the intricate structure of fibril-laden interfaces with their macroscopic adsorption kinetics and viscoelasticity. A subtle change in solution pH provokes pronounced changes in interfacial properties such as alignment, entanglement, multilayer formation, and fibril fracture, which can be resolved and linked across the various length scales involved |
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Beschreibung: | Date Completed 12.05.2015 Date Revised 26.08.2014 published: Print-Electronic Citation Status MEDLINE |
ISSN: | 1520-5827 |
DOI: | 10.1021/la5020658 |