Journal article
Aβ1-28 Fragment of the Amyloid Peptide Predominantly Adopts a Polyproline II Conformation in an Acidic Solution
Biochemistry (Easton), v 43(22), pp 6893-6898
08 Jun 2004
PMID: 15170326
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
To structurally characterize the nonaggregated state of the amyloid β peptide, which assembles into the hallmark fibrils of Alzheimer disease, we investigated the conformation of the N-terminal extracellular peptide fragment Aβ1-28 in D2O at acidic pD by utilizing combined FTIR and isotropic and anisotropic Raman spectra measured between 1550 and 1750 cm-1. Peptide aggregation is avoided under the conditions chosen. The amide I‘ band was found to exhibit a significant noncoincidence effect in that the first moment of the anisotropic Raman and of the IR band profile appears red-shifted from that of the isotropic Raman scattering. A simulation based on a coupled oscillator model involving all 27 amide I‘ modes of the peptide reveals that the peptide adopts a predominantly polyproline II conformation. Our results are inconsistent with the notion that the monomeric form of Aβ1-28 is a totally disordered, random-coil structure. Generally, they underscore the notion that polyproline II is a characteristic motif of the unfolded state of proteins and peptides.
Metrics
13 Record Views
Details
- Title
- Aβ1-28 Fragment of the Amyloid Peptide Predominantly Adopts a Polyproline II Conformation in an Acidic Solution
- Creators
- Fatma Eker - Departments of Chemistry and Biology, University of Puerto Rico, Río Piedras Campus, P.O. Box 23346, San Juan PR00931,Puerto Rico, and Department of Chemistry, Drexel University, Philadelphia, Pennsylvania 19104Kai Griebenow - Departments of Chemistry and Biology, University of Puerto Rico, Río Piedras Campus, P.O. Box 23346, San Juan PR00931,Puerto Rico, and Department of Chemistry, Drexel University, Philadelphia, Pennsylvania 19104Reinhard Schweitzer-Stenner - Drexel University, Chemistry
- Publication Details
- Biochemistry (Easton), v 43(22), pp 6893-6898
- Publisher
- American Chemical Society
- Number of pages
- 6
- Grant note
- NCRR NIH HHS: P20 RR16439-01
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Web of Science ID
- WOS:000221807500007
- Scopus ID
- 2-s2.0-2642567722
- Other Identifier
- 991019167947104721
UN Sustainable Development Goals (SDGs)
This publication has contributed to the advancement of the following goals:
InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology