Effect of Ala-substitution, N- and C-terminal modification and the presence of counter ions on the structure of amyloid peptide fragment 25-35

Tamás Körtvélyesi, Gergo Kiss, Richard F. Murphy, Botond Penke, Sándor Lovas

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The effect of the Ala-substitution, the N- and C-terminal capping and the presence of Ca2+, Mg2+ and Zn2+ on the structure of amyloid peptide fragment, Aβ(25-35), and its analog, [Ala31,32,34,35]Aβ(25-35), was studied. One nanosecond NPT molecular dynamics simulation was used to examine the structural stability of the peptides in water. Calculations were performed using the modified GROMOS-87 force field with SPC/E water model, applying the weak temperature and pressure coupling method. During the simulation of the Aβ(25-35) structure, an initial helical structure was destroyed. In Ac-[Ala31,32,34,35]Aβ(25-35)-NHCH3, however, the helix was stable and even more so in the presence of Ca2+, Mg2+ and Zn2+ cations. Between residues 27 and 34, mainly turn/bend and less frequently helix, respectively, characterized the secondary structure of Aβ(25-35) and [Ala31,32,34,35]Aβ(25-35).

Original languageEnglish
Pages (from-to)215-223
Number of pages9
JournalJournal of Molecular Structure: THEOCHEM
Volume545
DOIs
StatePublished - Jul 9 2001

Fingerprint

Peptide Fragments
Radiation counters
Amyloid
helices
Peptides
peptides
counters
Substitution reactions
fragments
Ions
substitutes
Water
structural stability
Molecular Dynamics Simulation
water
field theory (physics)
Molecular dynamics
Cations
ions
simulation

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Computational Theory and Mathematics
  • Atomic and Molecular Physics, and Optics

Cite this

Effect of Ala-substitution, N- and C-terminal modification and the presence of counter ions on the structure of amyloid peptide fragment 25-35. / Körtvélyesi, Tamás; Kiss, Gergo; Murphy, Richard F.; Penke, Botond; Lovas, Sándor.

In: Journal of Molecular Structure: THEOCHEM, Vol. 545, 09.07.2001, p. 215-223.

Research output: Contribution to journalArticle

@article{f54b43d5c6fa401db4ee7a90d8f694e6,
title = "Effect of Ala-substitution, N- and C-terminal modification and the presence of counter ions on the structure of amyloid peptide fragment 25-35",
abstract = "The effect of the Ala-substitution, the N- and C-terminal capping and the presence of Ca2+, Mg2+ and Zn2+ on the structure of amyloid peptide fragment, Aβ(25-35), and its analog, [Ala31,32,34,35]Aβ(25-35), was studied. One nanosecond NPT molecular dynamics simulation was used to examine the structural stability of the peptides in water. Calculations were performed using the modified GROMOS-87 force field with SPC/E water model, applying the weak temperature and pressure coupling method. During the simulation of the Aβ(25-35) structure, an initial helical structure was destroyed. In Ac-[Ala31,32,34,35]Aβ(25-35)-NHCH3, however, the helix was stable and even more so in the presence of Ca2+, Mg2+ and Zn2+ cations. Between residues 27 and 34, mainly turn/bend and less frequently helix, respectively, characterized the secondary structure of Aβ(25-35) and [Ala31,32,34,35]Aβ(25-35).",
author = "Tam{\'a}s K{\"o}rtv{\'e}lyesi and Gergo Kiss and Murphy, {Richard F.} and Botond Penke and S{\'a}ndor Lovas",
year = "2001",
month = "7",
day = "9",
doi = "10.1016/S0166-1280(01)00422-5",
language = "English",
volume = "545",
pages = "215--223",
journal = "Computational and Theoretical Chemistry",
issn = "2210-271X",
publisher = "Elsevier BV",

}

TY - JOUR

T1 - Effect of Ala-substitution, N- and C-terminal modification and the presence of counter ions on the structure of amyloid peptide fragment 25-35

AU - Körtvélyesi, Tamás

AU - Kiss, Gergo

AU - Murphy, Richard F.

AU - Penke, Botond

AU - Lovas, Sándor

PY - 2001/7/9

Y1 - 2001/7/9

N2 - The effect of the Ala-substitution, the N- and C-terminal capping and the presence of Ca2+, Mg2+ and Zn2+ on the structure of amyloid peptide fragment, Aβ(25-35), and its analog, [Ala31,32,34,35]Aβ(25-35), was studied. One nanosecond NPT molecular dynamics simulation was used to examine the structural stability of the peptides in water. Calculations were performed using the modified GROMOS-87 force field with SPC/E water model, applying the weak temperature and pressure coupling method. During the simulation of the Aβ(25-35) structure, an initial helical structure was destroyed. In Ac-[Ala31,32,34,35]Aβ(25-35)-NHCH3, however, the helix was stable and even more so in the presence of Ca2+, Mg2+ and Zn2+ cations. Between residues 27 and 34, mainly turn/bend and less frequently helix, respectively, characterized the secondary structure of Aβ(25-35) and [Ala31,32,34,35]Aβ(25-35).

AB - The effect of the Ala-substitution, the N- and C-terminal capping and the presence of Ca2+, Mg2+ and Zn2+ on the structure of amyloid peptide fragment, Aβ(25-35), and its analog, [Ala31,32,34,35]Aβ(25-35), was studied. One nanosecond NPT molecular dynamics simulation was used to examine the structural stability of the peptides in water. Calculations were performed using the modified GROMOS-87 force field with SPC/E water model, applying the weak temperature and pressure coupling method. During the simulation of the Aβ(25-35) structure, an initial helical structure was destroyed. In Ac-[Ala31,32,34,35]Aβ(25-35)-NHCH3, however, the helix was stable and even more so in the presence of Ca2+, Mg2+ and Zn2+ cations. Between residues 27 and 34, mainly turn/bend and less frequently helix, respectively, characterized the secondary structure of Aβ(25-35) and [Ala31,32,34,35]Aβ(25-35).

UR - http://www.scopus.com/inward/record.url?scp=0035832699&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035832699&partnerID=8YFLogxK

U2 - 10.1016/S0166-1280(01)00422-5

DO - 10.1016/S0166-1280(01)00422-5

M3 - Article

AN - SCOPUS:0035832699

VL - 545

SP - 215

EP - 223

JO - Computational and Theoretical Chemistry

JF - Computational and Theoretical Chemistry

SN - 2210-271X

ER -