NDLI: Quantitative Characterization of Protein Nanostructures Using Atomic Force Microscopy

Content Provider	IEEE Xplore Digital Library
Author	Segers-Nolten, I. van der Werf, K. van Raaij, M. Subramaniam, V.
Copyright Year	2007
Description	Author affiliation: Univ. of Twente, Enschede (Segers-Nolten, I.; van der Werf, K.; van Raaij, M.; Subramaniam, V.)
Abstract	The aggregation of proteins into fibrillar structures called amyloid is a characteristic of many diseases, including several neurodegenerative disorders. Although amyloid formation is inherent to several serious diseases, the mechanism of fibril formation and the modes of toxicity are not yet known. High concentrations of fibrillar aggregates of alpha-synuclein protein are found in the brains of patients suffering from Parkinson's disease. We exploit different contrast modes of high resolution atomic force microscopy (AFM) on fibrils formed by the wild-type alpha-synuclein protein, and by the familial disease-related A30P, E46K and A53T variants, to get more insight into the in vitro process of fibril assembly. From quantitative analysis of height images measured in tapping mode AFM, we obtained data that are compatible with a twisted hierarchical assembly model [1] for all protein variants. The E46K mutant displays the most distinct and smallest periodicity. The modulation depth for all mutants is very similar, and is smaller for wild-type protein commensurate with the lower fibril height. The detailed morphology observed in phase images indicates however that fibrils may also be formed through the association of fibril segments. To study the mechanical properties of fibrils we applied force while scanning in contact mode, resulting in characteristic deformation of protein fibrils with a periodicity corresponding to the modulation observed in tapping mode. Our observations suggest that the hierarchical assembly model may not be the exclusive mechanism of alpha-synuclein fibril assembly, but that multiple modes of fibril assembly play a role in alpha-synuclein fibril formation.
Starting Page	6608
Ending Page	6611
File Size	471247
Page Count	4
File Format	PDF
ISBN	9781424407873
ISSN	1557170X
DOI	10.1109/IEMBS.2007.4353874
Language	English
Publisher	Institute of Electrical and Electronics Engineers, Inc. (IEEE)
Publisher Date	2007-08-22
Publisher Place	France
Access Restriction	Subscribed
Rights Holder	Institute of Electrical and Electronics Engineers, Inc. (IEEE)
Subject Keyword	Atomic force microscopy Proteins Nanostructures Assembly Parkinson's disease Aggregates Atomic measurements In vitro Image analysis Displays
Content Type	Text
Resource Type	Article
Subject	Signal Processing Biomedical Engineering Health Informatics Computer Vision and Pattern Recognition

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in