Template-directed self-assembly and growth of insulin amyloid fibrils
Template-directed self-assembly and growth of insulin amyloid fibrils
Engineering Village 2
? 2006 Elsevier Inc
Accession number: 05249150293
Title: Template-directed self-assembly and growth of insulin amyloid fibrils
Authors: Ha, Chanki; Park, Chan Beum
Author affiliation: Department of Chemical and Materials Engineering and Science and Engineering of Materials Program, Arizona State University, Tempe, AZ 85287, United States
Serial title: Biotechnology and Bioengineering
Abbreviated serial title: Biotechnol. Bioeng.
Volume: v 90
Issue: n 7
Issue date: Jun 30 2005
Publication year: 2005
Pages: p 848-855
Language: English
ISSN: 0006-3592
CODEN: BIBIAU
Document type: Journal article (JA)
Publisher: John Wiley and Sons Inc., Newark, NJ 07191-8667, United States
Abstract: The formation of amyloid aggregates in tissue is a pathological feature of many neurodegenerative diseases and type II diabetes. Amyloid deposition, the process of amyloid growth by the association of individual soluble amyloid molecules with a pre-existing amyloid template (i.e., plaque), is known to be critical for amyloid formation in vivo. The requirement for a natural amyloid template, however, has made amyloid deposition study difficult and cumbersome. In the present work, we developed a novel, synthetic amyloid template by attaching amyloid seeds covalently onto an N-hydroxy-succinimide-activated surface, where insulin was chosen as a model amyloidogenic protein. According to ex situ atomic force microscopy observations, insulin monomers in solution were deposited onto the synthetic amyloid template to form fibrils, like hair growth. The fibril formation on the template occurred without lag time, and its rate was highly accelerated than in the solution. The fibrils were long, over 2 ?m, and much thinner than those in the solution, which was caused by limited nucleation sites on the template surface and lack of lateral twisting between fibrils. According to our investigations using thioflavin T-induced fluorescence, birefringent Congo red binding, and circular dichroism, fibrils grown on the template were identified to be amyloids that formed through a conformational rearrangement of insulin monomers upon interaction with the template. The amyloid deposition rate followed saturation kinetics with respect to insulin concentration in the solution. The characteristics of amyloid deposition on the synthetic template were in agreement with previous studies performed with human amyloid plaques. It is demonstrated that the synthetic amyloid template can be used for the screening of inhibitors on amyloid deposition in vitro. ? 2005 Wiley Periodicals, Inc.
Number of references: 39
Ei main heading: Tissue
Ei controlled terms: Insulin - Growth kinetics - Self assembly - Pathology - Diseases - Neurology - Deposition - Proteins - Nucleation - Fluorescence - Monomers - Screening - Atomic force microscopy
Uncontrolled terms: Insulin amyloid fibrils - Neurodegenerative diseases - Circular dichroism - Insulin monomers
Ei classification codes: 461.2 Biological Materials - 461.8 Biotechnology - 461.6 Medicine - 804.1 Organic Compounds - 933.1.2 Crystal Growth - 741.1 Light/Optics - 802.3 Chemical Operations - 741.3 Optical Devices & Systems
Treatment: Experimental (EXP)
DOI: 10.1002/bit.20486
Database: Compendex
Compilation and indexing terms, ? 2006 Elsevier Inc. All rights reserved
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