한빛사논문
- 조회2,153
Abstract
Seung-gu Kang†, Hai Li ‡, Tien Huynh †, Fuchun Zhang ‡, Zhen Xia †§, Yi Zhang ‡*, and Ruhong Zhou †⊥*
† Computational Biology Center, IBM Thomas J. Watson Research Center, Yorktown Heights, New York 10598, United States
‡ Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai 201800, China
§ Department of Biomedical Engineering, The University of Texas at Austin, Austin, Texas 78712, United States
⊥ Department of Chemistry, Columbia University, New York, New York 10027, United States
*Address correspondence to Yi Zhang, Ruhong Zhou
Abstract
A surprising “upright” fibrilar conformation (with a height of ~2.6 nm) was observed with in situ atomic force microscopy (AFM) for an amyloid-like peptide (NH2-VGGAVVAV-COHN2) on mica surface, which is very different from its “flat” conformation (with a much smaller height of ~0.9 nm) on the HOPG surface. Our all-atom molecular dynamics (MD) simulations reveal that it is the strong electrostatic interactions between the N-terminus of the peptide and the mica surface that result in an upright conformation and a highly ordered β-stranded structure on mica, with a height of 2.5 ± 0.1 nm, consistent with the AFM experiment. Similarly, our MD simulations show that the same peptides adopt a flat conformation on HOPG surfaces due to the favorable hydrophobic interactions with HOPG. Our simulations also indicate that epitaxial patterns found in mica are preferentially controlled by anisotropic binding sites commensurate with the inherent crystallographic unit cell of the basal substrate.
Keywords: peptide self-assembly; muscovite mica; epitaxial growth; amyloid peptide; molecular dynamics simulation
논문정보
- Research article
- 2012년 09월 (BRIC 등록일 )
- 국외 연구진
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