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Graphite-Templated Amyloid Nanostructures Formed by a Potential Pentapeptide Inhibitor for Alzheimer's Disease: A Combined Study of Real-Time Atomic Force Microscopy and Molecular Dynamics Simulations

  1. Author:
    Li, Na
    Jang, Hyunbum
    Yuan, Ming
    Li, Wanrong
    Yun, Xiaolin
    Lee, Joon
    Du, Qiqige
    Nussinov, Ruth
    Hou, Jiahua
    Lal, Ratnesh
    Zhang, Feng

  2. Author Address

    Inner Mongolia Agr Univ, Sch Life Sci, Agr Nanoctr, 306 Zhaowuda Rd, Hohhot 010018, Peoples R China.Leidos Biomed Res Inc, Frederick Natl Lab Canc Res, Natl Canc Inst Frederick, Canc & Inflammat Program, Frederick, MD 21702 USA.Univ Calif San Diego, Mat Sci & Engn Program, 9500 Gilman Dr, La Jolla, CA 92093 USA.Univ Calif San Diego, Dept Mech & Aerosp Engn, 9500 Gilman Dr, La Jolla, CA 92093 USA.Univ Calif San Diego, Dept Bioengn, 9500 Gilman Dr, La Jolla, CA 92093 USA.Tel Aviv Univ, Sadder Sch Med, Dept Human Mol Genet & Biochem, IL-69978 Tel Aviv, Israel.Guangzhou Med Univ, Sch Basic Med Sci, Dept Biomed Engn, Guangzhou 511436, Guangdong, Peoples R China.
    1. Year: 2017
    2. Date: Jul 11
    3. Epub Date: 2017 Jun 12
  2. Journal: Langmuir
  3. AMER CHEMICAL SOC,
    1. 33
    2. 27
    3. Pages: 6647-6656
  5. Type of Article: Article
  6. ISSN: 0743-7463
  1. Abstract:

    Self-assembly of peptides is closely related to many diseases, including Alzheimer's, Parkinson's, and prion diseases. Understanding the basic mechanism of this assembly is essential for designing ultimate cure and preventive measures. Template-assisted self-assembly (TASA) of peptides on inorganic substrates can provide fundamental under-standing of substrate-dependent peptides assemble, including the role of hydrophobic interface on the peptide fibrillization. Here, we have studied the self-assembly process of a potential pentapeptide inhibitor on the surface of highly oriented pyrolytic graphite (HOPG) using real time atomic force microscopy (RT-AFM) as well as molecular dynamics (MD) simulation. Experimental and simulation results show nanofilament formation consisting of beta-sheet structures and epitaxial growth on HOPG. Height analysis of the nanofilaments and MD simulation indicate that the peptides adopt a lying down configuration of double-layered antiparallel beta-sheets for its epitaxial growth, and the number of nanofilament layers is concentration-dependent. These findings provide new perspective for the mechanism of peptide-based fibrillization in amyloid diseases as well as for designing well-ordered micrometrical and nanometrical structures.

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External Sources

  1. View Full Text
  2. DOI: 10.1021/acs.langmuir.7b00414
  3. PMID: 28605901
  4. View record in Web of Science®
  5. WOS: 000405536100002

Library Notes

  1. Fiscal Year: FY2016-2017
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