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Turn-Directed α-β Conformational Transition of α-syn12 Peptide at Different pH Revealed by Unbiased Molecular Dynamics Simulations
Department of Computer Science and Technology, Dezhou University, Dezhou 253023, China
Shandong Provincial Key Laboratory of Functional Macromolecular Biophysics, Dezhou 253023, China
* Author to whom correspondence should be addressed.
Received: 25 February 2013; in revised form: 24 April 2013 / Accepted: 24 April 2013 / Published: 24 May 2013
Abstract: The transition from α-helical to β-hairpin conformations of α-syn12 peptide is characterized here using long timescale, unbiased molecular dynamics (MD) simulations in explicit solvent models at physiological and acidic pH values. Four independent normal MD trajectories, each 2500 ns, are performed at 300 K using the GROMOS 43A1 force field and SPC water model. The most clustered structures at both pH values are β-hairpin but with different turns and hydrogen bonds. Turn9-6 and four hydrogen bonds (HB9-6, HB6-9, HB11-4 and HB4-11) are formed at physiological pH; turn8-5 and five hydrogen bonds (HB8-5, HB5-8, HB10-3, HB3-10 and HB12-1) are formed at acidic pH. A common folding mechanism is observed: the formation of the turn is always before the formation of the hydrogen bonds, which means the turn is always found to be the major determinant in initiating the transition process. Furthermore, two transition paths are observed at physiological pH. One of the transition paths tends to form the most-clustered turn and improper hydrogen bonds at the beginning, and then form the most-clustered hydrogen bonds. Another transition path tends to form the most-clustered turn, and turn5-2 firstly, followed by the formation of part hydrogen bonds, then turn5-2 is extended and more hydrogen bonds are formed. The transition path at acidic pH is as the same as the first path described at physiological pH.
Keywords: Parkinson’s disease; α-syn12 peptide; α-β transition mechanism; different pH
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Liu, L.; Cao, Z. Turn-Directed α-β Conformational Transition of α-syn12 Peptide at Different pH Revealed by Unbiased Molecular Dynamics Simulations. Int. J. Mol. Sci. 2013, 14, 10896-10907.
Liu L, Cao Z. Turn-Directed α-β Conformational Transition of α-syn12 Peptide at Different pH Revealed by Unbiased Molecular Dynamics Simulations. International Journal of Molecular Sciences. 2013; 14(6):10896-10907.
Liu, Lei; Cao, Zanxia. 2013. "Turn-Directed α-β Conformational Transition of α-syn12 Peptide at Different pH Revealed by Unbiased Molecular Dynamics Simulations." Int. J. Mol. Sci. 14, no. 6: 10896-10907.