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Title: Self-assembly of A{Beta}{sub 10--35}-PEG block copolymer fibrils

Abstract

{beta}-sheet secondary structure is energetically dependent not only on the H-bonding interactions between individual strands, but also on the ability of the resulting sheet to twist, bulge, and fold into multifaceted macromolecular conformations. Consequently, amino acid propensities have proven to be highly context-dependent, greatly complicating the design of peptides and proteins rich in {beta}-structure. Most problematic, however, are the intermolecular interactions which compromise solubility, the infamous feature of the many amyloid diseases. The authors have exploited the energetics of self-association of amyloid peptides in the construction of a block copolymer consisting of the central domain from the {beta}-amyloid peptide conjugated with poly(ethylene glycol) at the C-terminus, 1. This paper uses small angle neutron scattering (SANS) and electron microscopy (EM), to demonstrate the location and disposition of the PEG block to be on the surface of the fibril, ensuring the solubility of the fibrillar copolymer.

Authors:
; ; ; ; ;
Publication Date:
Research Org.:
Argonne National Lab., IL (US)
Sponsoring Org.:
National Institutes of Health (NIH); USDOE
OSTI Identifier:
20000036
DOE Contract Number:  
W-31109-ENG-38
Resource Type:
Journal Article
Journal Name:
Journal of the American Chemical Society
Additional Journal Information:
Journal Volume: 121; Journal Issue: 32; Other Information: PBD: 18 Aug 1999; Journal ID: ISSN 0002-7863
Country of Publication:
United States
Language:
English
Subject:
55 BIOLOGY AND MEDICINE, BASIC STUDIES; PEPTIDES; POLYETHYLENE GLYCOLS; COPOLYMERS; ELECTRON MICROSCOPY; PROTEIN STRUCTURE

Citation Formats

Burkoth, T.S., Benzinger, T.L.S., Urban, V., Lynn, D.G., Meredith, S.C., and Thiyagarajan, P. Self-assembly of A{Beta}{sub 10--35}-PEG block copolymer fibrils. United States: N. p., 1999. Web. doi:10.1021/ja991233x.
Burkoth, T.S., Benzinger, T.L.S., Urban, V., Lynn, D.G., Meredith, S.C., & Thiyagarajan, P. Self-assembly of A{Beta}{sub 10--35}-PEG block copolymer fibrils. United States. doi:10.1021/ja991233x.
Burkoth, T.S., Benzinger, T.L.S., Urban, V., Lynn, D.G., Meredith, S.C., and Thiyagarajan, P. Wed . "Self-assembly of A{Beta}{sub 10--35}-PEG block copolymer fibrils". United States. doi:10.1021/ja991233x.
@article{osti_20000036,
title = {Self-assembly of A{Beta}{sub 10--35}-PEG block copolymer fibrils},
author = {Burkoth, T.S. and Benzinger, T.L.S. and Urban, V. and Lynn, D.G. and Meredith, S.C. and Thiyagarajan, P.},
abstractNote = {{beta}-sheet secondary structure is energetically dependent not only on the H-bonding interactions between individual strands, but also on the ability of the resulting sheet to twist, bulge, and fold into multifaceted macromolecular conformations. Consequently, amino acid propensities have proven to be highly context-dependent, greatly complicating the design of peptides and proteins rich in {beta}-structure. Most problematic, however, are the intermolecular interactions which compromise solubility, the infamous feature of the many amyloid diseases. The authors have exploited the energetics of self-association of amyloid peptides in the construction of a block copolymer consisting of the central domain from the {beta}-amyloid peptide conjugated with poly(ethylene glycol) at the C-terminus, 1. This paper uses small angle neutron scattering (SANS) and electron microscopy (EM), to demonstrate the location and disposition of the PEG block to be on the surface of the fibril, ensuring the solubility of the fibrillar copolymer.},
doi = {10.1021/ja991233x},
journal = {Journal of the American Chemical Society},
issn = {0002-7863},
number = 32,
volume = 121,
place = {United States},
year = {1999},
month = {8}
}