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
N1 - Funding Information:
This work was supported by the State of Nebraska Department of Health, Cancer and Smoking related Disease Research Program LB595 and Carpenter Chair in Biochemistry, Creighton University (S.L., R.F.M. and T.K.) and the Hungarian Research Fund (G.K. and B.P., OTKA TO34895/1999).
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).
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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
IS - 1-3
ER -