𝔖 Bobbio Scriptorium
✦   LIBER   ✦

15N relaxation study of the amyloid β-peptide: structural propensities and persistence length

✍ Scribed by Jens Danielsson; August Andersson; Jüri Jarvet; Astrid Gräslund

Publisher
John Wiley and Sons
Year
2006
Tongue
English
Weight
410 KB
Volume
44
Category
Article
ISSN
0749-1581

No coin nor oath required. For personal study only.

✦ Synopsis

The dynamics of monomeric Alzheimer Abeta1-40 in aqueous solution was studied using heteronuclear NMR experiments. 15N NMR relaxation rates of amide groups report on the dynamics in the peptide chain and make it possible to estimate structural propensities from temperature-dependent relaxation data and chemical shifts change analysis. The persistence length of the polypeptide chain was determined using a model in which the influence of neighboring residue relaxation is assumed to decay exponentially as a function of distance. The persistence length of the Abeta1-40 monomer was found to decrease from eight to three residues when temperature was increased from 3 to 18 degrees C. At 3 degrees C the peptide shows structural propensities that correlate well with the suggested secondary structure regions of the peptide to be present in the fibrils, and with the alpha-helical structure in membrane-mimicking systems. Our data leads to a structural model for the monomeric soluble beta-peptide with six different regions of secondary structure propensities. The peptide has two regions with beta-strand propensity (residues 16-24 and 31-40), two regions with high PII-helix propensity (residues 1-4 and 11-15) and two unstructured regions with higher mobility (residues 5-10 and 25-30) connecting the structural elements.

📜 SIMILAR VOLUMES

Structural and dynamical analysis of the
Structural and dynamical analysis of the hydration of the Alzheimer's β-amyloid peptide
✍ Francesca Massi; John E. Straub 📂 Article 📅 2002 🏛 John Wiley and Sons 🌐 English ⚖ 451 KB 👁 1 views

An analysis of the water molecules in the first solvation shell obtained from the molecular dynamics simulation of the amyloid beta(10-35)NH2 peptide and the amyloid beta(10-35)NH2E22Q "Dutch" mutant peptide is presented. The structure, energetics, and dynamics of water in the hydration shell have b

Design of a Peptide Undergoing α–β Struc
Design of a Peptide Undergoing α–β Structural Transition and Amyloid Fibrillogenesis by the Introduction of a Hydrophobic Defect
✍ Yuta Takahashi; Akihiko Ueno; Hisakazu Mihara 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 314 KB 👁 1 views

An improved understanding of protein misfolding is critical to the study of proteins involved in diseases such as Alzheimers and prion-related diseases, as well as to the clarification of the folding pathway of proteins. In general, hydrophobic clustering seems to be an important feature for peptide

Study of the non-covalent interaction be
Study of the non-covalent interaction between amyloid-β-peptide and melatonin using electrospray ionization mass spectrometry
✍ Fotini N. Bazoti; Anthony Tsarbopoulos; Karin E. Markides; Jonas Bergquist 📂 Article 📅 2005 🏛 John Wiley and Sons 🌐 English ⚖ 337 KB 👁 1 views

## Abstract Oxidative stress and unregulated immune response are believed to play a key role in the processes inherent to Alzheimer's disease (AD). The fact that free radicals can result in neurodegeneration suggests that actions against reactive oxygen species may be beneficial in treating and pre

Hydrolysis of the amyloid β-peptide (Aβ)
Hydrolysis of the amyloid β-peptide (Aβ) 1–40 between Asp23–Val24 produces non-aggregating fragments. An electrospray mass spectrometric study
✍ Waltteri Hosia; William J. Griffiths; Jan Johansson 📂 Article 📅 2005 🏛 John Wiley and Sons 🌐 English ⚖ 108 KB 👁 1 views

## Abstract The aggregation of full‐length (residues 1–40) amyloid β‐peptide (Aβ) and fragments corresponding to residues 1–23 and 24–40 was studied by electrospray mass spectrometry, using gramicidin as a non‐aggregating reference. Following a lag period, Aβ(1–40) at 140 µM concentration aggregate