Nuclear Science and Techniques

《核技术》(英文版) ISSN 1001-8042 CN 31-1559/TL     2019 Impact factor 1.556

Nuclear Science and Techniques ›› 2019, Vol. 30 ›› Issue (8): 117 doi: 10.1007/s41365-019-0645-8


In Situ AFM investigation of dual-mode self-assembling peptide

Yue-Xian Bao1, Ming Yuan2, Qiqige Du3, Yu-Bo Li2, Jing-Yu Gao2, Abdul Jamil Khan2, Feng Zhang1, 2, 4   

  1. 1 College of Animal Science, Inner Mongolia Agricultural University, 306 Zhaowuda Road, Hohhot 010018, China
    2 Biomedical Nanocenter, School of Life Science, Inner Mongolia Agricultural University, 29 East Erdos Street, Hohhot 010011, China
    3 State Key Laboratory of Molecular Engineering of Polymers and Department of Macromolecular Science, Fudan University, 220 Handan Road, Shanghai 200433, China
    4 Key Laboratory of Oral Medicine, Guangzhou Institute of Oral Disease, Stomatology Hospital, Department of Biomedical Engineering, School of Basic Medical Sciences, Guangzhou Medical University, Guangzhou 511436, China
  • Received:2019-04-08 Revised:2019-05-15 Accepted:2019-05-23
  • Contact: Feng Zhang
  • Supported by:
    This work was supported by the following programs and foundations: the Program Funded by the University for Fostering Distinguished Young Scholars, the National Natural Science Foundation of China (No. 51763019, U1832125), the China Postdoctoral Science Foundation (No. 2018M630937), the Grassland Talents Program of Inner Mongolia Autonomous Region, the Distinguished Young Scholars Foundation of Inner Mongolia Autonomous Region, and the Young Leading Talents of Science and Technology Program of Inner Mongolia Autonomous Region.
PDF ShareIt Export Citation
Yue-Xian Bao, Ming Yuan, Qiqige Du, Yu-Bo Li, Jing-Yu Gao, Abdul Jamil Khan, Feng Zhang. In Situ AFM investigation of dual-mode self-assembling peptide.Nuclear Science and Techniques, 2019, 30(8): 117     doi: 10.1007/s41365-019-0645-8

Abstract: Nano-structures/patterns formed by biomolecules can produce different physicochemical properties in terms of hydrophobicity, zeta-potential, color, etc., which play paramount roles in life. Peptides, as the main bio-building blocks, can form nanostructures with different functions, either in solutions or on interfaces. Previously, we synthesized a short peptide with the inspiration of an Alzheimer’s disease (AD) related peptide: amyloid β peptide (A-β), namely GAV-9, which can epitaxially self-assemble into regular nanofilaments on liquid–solid interfaces, and it was found that both the hydrophobicity and charge state of the interfaces can significantly influence its assembling behavior. It was also reported that another A-β contained dipeptide, FF, can self-assemble into nanostructures in solutions. Owing to the close relationship between these two short peptides, it is interesting to conjugate them into a de novo peptide with two separated structural domains and study its self-assembling behavior. To this end, herein we have synthesized the GAV-FF peptide with a sequence of NH2-VGGAVVAGVFF-CONH2, and verified its self-assembling property using the in situ liquid phase atomic force microscopy (AFM). The results show that the GAV-FF peptide can self-assemble into nanofilaments both in solutions and on aqueous–solid interfaces, but with different morphologies. The FF domain accelerates the template-assisted self-assembling (TASA) process of the GAV domain, which in return enhances the solubility of FF in aqueous solutions and further participates in the fibrillization of FF. The current results could help deepen the understanding of the aggregation mechanism of disease-related peptides, and could also shed light on the strategies to create artificial bio-functional nanostructures/patterns, which hold a significant potential for biomedical applications.

Key words: Amyloid peptide, Nanofilament, Self-assembly, Structural domain, Atomic force microscopy