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 language | English |
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Pages (from-to) | 215-223 |
Number of pages | 9 |
Journal | Journal of Molecular Structure: THEOCHEM |
Volume | 545 |
DOIs | |
State | Published - Jul 9 2001 |
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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 journal › Article
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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 -