A Novel Method to Measure the Effective Change of the Interfacial Energy due to Kinetic Self-Assembly of Amyloid Fibrils

被引:1
|
作者
Lin, Yi-Chih [1 ]
Skolnick, Murray [1 ]
Fakhraai, Zahra [1 ]
机构
[1] Univ Penn, Dept Chem, 231 South 34th St, Philadelphia, PA 19104 USA
来源
JOURNAL OF PHYSICAL CHEMISTRY B | 2019年 / 123卷 / 32期
关键词
SURFACE; FILMS; MODEL;
D O I
10.1021/acs.jpcb.9b04717
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Adsorbates growing a self-assembled layer on a solid-liquid interface can significantly change the effective interfacial energy at the solid surface. However, measuring the changes in the effective surface energy while these adsorbates accumulate is challenging, as static contact angle measurements can be affected by the motion and accumulation of these adsorbates at the droplet's boundary (coffee stain effects). In this report, we utilize a novel method that takes advantage of spin-induced dewetting to measure the change in the effective surface energy as the self-assembly progresses. We use a previously well-studied model system of self-assembled fibrils of amyloid-beta (A beta) peptides on the mica substrate to demonstrate the feasibility of this method. Using variations of terminal spin speeds and acceleration rates, we measure the terminal spin speed at which a wetting-dewetting transition (WDT) occurs on a surface that hosts self-assembled A beta(12-28) fibrils. By comparing this speed with the WDT speed on the bare mica substrate, we can quantify the spreading coefficient and thus the effective change of the substrate's interfacial energy due to the adsorption of mobile peptides at various stages of the self-assembly. These measurements show that the surface becomes more hydrophilic as the self-assembly progresses and thus can explain previous observations that the self-assembly of this particular peptide system is self-limiting and stops before full surface coverage.
引用
收藏
页码:6990 / 6996
页数:7
相关论文
共 50 条
  • [21] Scanning Tunneling Microscopy Reveals Single-Molecule Insights into the Self-Assembly of Amyloid Fibrils
    Kalashnyk, Nataliya
    Nielsen, Jakob T.
    Nielsen, Erik H.
    Skrydstrup, Troels
    Otzen, Daniel E.
    Laegsgaard, Erik
    Wang, Chen
    Besenbacher, Flemming
    Nielsen, Niels Chr
    Linderoth, Trolle R.
    ACS NANO, 2012, 6 (08) : 6882 - 6889
  • [22] Modeling the Effect of Monomer Conformational Change on the Early Stage of Protein Self-Assembly into Fibrils
    Kashchiev, Dimo
    JOURNAL OF PHYSICAL CHEMISTRY B, 2017, 121 (01): : 35 - 46
  • [23] Detailed Mechanism of Rapid Amyloid Fibril Self-Assembly Due to Surface Diffusion
    Lin, Yi-Chih
    Petersson, E. James
    Fakhraai, Zahra
    BIOPHYSICAL JOURNAL, 2015, 108 (02) : 523A - 523A
  • [24] ANYL 176-Nanostructured interfacial self-assembly of an amyloid-like peptide
    Guenoun, Patrick
    Chevallard, Corinne
    Lepere, Mathilde
    Brezesinski, Gerald
    Goldmann, Michel
    Muenter, Annabel H.
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2008, 235
  • [25] Identification of a subunit interface in transthyretin amyloid fibrils: Evidence for self-assembly from oligomeric building blocks
    Serag, AA
    Altenbach, C
    Gingery, M
    Hubbell, WL
    Yeates, TO
    BIOCHEMISTRY, 2001, 40 (31) : 9089 - 9096
  • [26] Interfacial self-assembly: A novel and facile strategy for nanofilm and nanodevice fabrication
    Hu Linfeng
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2014, 248
  • [27] Exploiting peptide self-assembly to engineer novel biopolymers: Tapes, ribbons, fibrils and fibres
    Aggeli, A
    Nyrkova, IA
    Bell, M
    Carrick, L
    McLeish, TCB
    Semenov, AN
    Boden, N
    SELF-ASSEMBLING PEPTIDE SYSTEMS IN BIOLOGY, MEDICINE AND ENGINEERING, 2001, : 1 - 17
  • [28] The Role of Protein Hydrophobicity in Conformation Change and Self-Assembly into Large Amyloid Fibers
    Ridgley, Devin M.
    Claunch, Elizabeth C.
    Lee, Parker W.
    Barone, Justin R.
    BIOMACROMOLECULES, 2014, 15 (04) : 1240 - 1247
  • [29] Hydrophobicity and Conformational Change as Mechanistic Determinants for Nonspecific Modulators of Amyloid β Self-Assembly
    Abelein, Axel
    Bolognesi, Benedetta
    Dobson, Christopher M.
    Graslund, Astrid
    Lendel, Christofer
    BIOCHEMISTRY, 2012, 51 (01) : 126 - 137
  • [30] Spectroscopic evidence for amyloid-like interfacial self-assembly of hydrophobin Sc3
    Butko, P
    Buford, JP
    Goodwin, JS
    Stroud, PA
    McCormick, CL
    Cannon, GC
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2001, 280 (01) : 212 - 215