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
  • [1] Interfacial Electrostatic Self-Assembly of Amyloid Fibrils into Multifunctional Protein Films
    Han, Yangyang
    Cao, Yiping
    Zhou, Jiangtao
    Yao, Yang
    Wu, Xiaodong
    Bolisetty, Sreenath
    Diener, Michael
    Handschin, Stephan
    Lu, Canhui
    Mezzenga, Raffaele
    ADVANCED SCIENCE, 2023, 10 (09)
  • [2] Molecular recognition and self-assembly of amyloid fibrils
    Gazit, E
    BIOPHYSICAL JOURNAL, 2003, 84 (02) : 154A - 154A
  • [3] Self-Assembly of Ovalbumin into Amyloid and Non-Amyloid Fibrils
    Lara, Cecile
    Gourdin-Bertin, Simon
    Adamcik, Jozef
    Bolisetty, Sreenath
    Mezzenga, Raffaele
    BIOMACROMOLECULES, 2012, 13 (12) : 4213 - 4221
  • [4] A possible role for π-stacking in the self-assembly of amyloid fibrils
    Gazit, E
    FASEB JOURNAL, 2002, 16 (01): : 77 - 83
  • [5] Structural insights into the self-assembly mechanism of amyloid fibrils
    Radford, Sheena E.
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2009, 238
  • [6] Self-Assembly of Amyloid Fibrils That Display Active Enzymes
    Zhou, Xiao-Ming
    Entwistle, Aiman
    Zhang, Hong
    Jackson, Antony P.
    Mason, Thomas O.
    Shimanovich, Ulyana
    Knowles, Tuomas P. J.
    Smith, Andrew T.
    Sawyer, Elizabeth B.
    Perrett, Sarah
    CHEMCATCHEM, 2014, 6 (07) : 1961 - 1968
  • [7] Self-assembly of penta-selenopeptides into amyloid fibrils
    Gokula, Ram P.
    Mahato, Jaladhar
    Singh, Harkesh B.
    Chowdhury, Arindam
    CHEMICAL COMMUNICATIONS, 2018, 54 (83) : 11697 - 11700
  • [8] Characterizing Kinetic Intermediate in Amyloid Self-Assembly
    Liang, Chen
    BIOPHYSICAL JOURNAL, 2015, 108 (02) : 524A - 524A
  • [9] Peptide Self-assembly: From Toxins to Amyloid Fibrils and Nanotubes
    Rawat, Anoop
    Nagaraj, Ramakrishnan
    CURRENT TOPICS IN MEDICINAL CHEMISTRY, 2014, 14 (06) : 740 - 746
  • [10] Self-assembly & applications of food-based amyloid fibrils
    Mezzenga, Raffaele
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2017, 254