Surface functionalization of fibers based on amyloid-like protein aggregation

被引：0
|
作者：
Wang, Haoyue [1 ]
Hu, Yaning [1 ]
Zhao, Jian [1 ,2 ,3 ]
Yang, Peng [1 ,2 ,3 ]
机构：
[1] Key Laboratory of Applied Surface and Colloid Chemistry, Ministry of Education, Shaanxi Normal University, Shaanxi, Xi'an,710119, China
[2] Xi'an Key Laboratory of Polymeric Soft Matter, Shaanxi Normal University, Shaanxi, Xi'an,710119, China
[3] Xi'an International Joint Research Center on Functional Fiber and Soft Smart Textile, Shaanxi Normal University, Shaanxi, Xi'an,710119, China
来源：
Fangzhi Xuebao/Journal of Textile Research | 2024年 / 45卷 / 08期
关键词：
Objective Flexible wearable smart fabric is one of the ideal forms of the next generation of flexible wearable devices; in which the functional fiber construction plays a crucial role. In order to address the issues related to current surface functionalization strategies for polymer fibers such as complex modification processes and poor coating stability; this study developed a fiber surface functionalization strategy based on protein amyloid-like aggregation. Method This strategy involves immersing polyester fibers in a lysozyme phase transition solution containing functional substances; which can form stable functional coatings on the fiber surface at room temperature. Silver nanoparticle coating-modified fibers and fabrics; quantum dot-modified fibers; and PEG-modified fibers and fabrics were prepared. During the preparation process; the disulfide bonds in the protein molecules are broken and the resulted unfolded molecular chains undergo amyloid-like aggregation to form protein nanocoatings containing functional units on the fiber surface. The electrical conductivity; antibacterial property; luminescence behavior; hydrophilicity and coating stability of the functional fibers and fabrics were characterized. Results Various functional polyester fibers were fabricated based on the amyloid-like protein aggregation. The proteinaceous coating with specific functions was easily formed on the fibers surface within a short time under ambient conditions; exhibiting exceptional interfacial adhesion to withstand bending stresses and prevent functional coating detachment during the prolonged usage. The silver nanoparticle coating-modified fiber was prepared by means of amyloid-like protein aggregation induced by metal ions. The results suggested that when the lysozyme concentration was 0.02 mg/mL; the silver nanoparticle coating-modified fiber had optimal electrical conductivity with a resistance of only 1. 39 Ω when length of fiber was 1 cm. It could withstand 37 tear-off cycles in a 3M tape test and showed no significant change in resistance after 20 000 bending cycles; indicating the high stability of the formed silver nanoparticle coating. Furthermore; the silver nanoparticle coating-modified polyester fabrics exhibited certain antibacterial activity. Therefore; silver nanoparticle coating-modified fibers can be used to prepare the conductive antibacterial textiles. Quantum dot-modified fibers exhibited fluorescence under UV irradiation and the fluorescence properties were closely related to the concentration of lysozyme. With the increase of lysozyme concentration; the fluorescence on the fiber surface first increased and then decreased. When the lysozyme concentration was 5 mg/mL; it had the strongest fluorescence intensity and maintained good stability with no significant decrease in fluorescence intensity after 10 000 bending tests. To improve the hydrophilicity of polyester fibers; the lysozyme-PEG conjugates were firstly synthesis. The lysozyme-PEG coating was formed on the fiber surface significantly improving its hydrophilicity; which was evaluated through the characterizations of water drop immersion and moisture permeability. It is demonstrated that water drop immersion time decreased from 24 s to 2. 5 s and moisture permeability increased from 4 500 g/(m 2 • d) to 5 800 g/(m 2 • d). Furthermore; the water drops immersion time and moisture permeability of PEG modified fabrics was less affected by the cycle of bending. Conclusion Inspired by the strong adhesion of protein amyloid structure in nature; functional nanocoatings on the surface of fibers were constructed successfully with high curvature based on the amyloid-like protein aggregation strategy. The strategy is simple; efficient; and environmentally friendly; and the coating function is highly adjustable by controlling the functional substances. Notably; the coating can adhere stably on the surface; effectively solving the coating debonding problem during long-term use. It provides a new method for fiber surface functionalization and has great application prospects in the field of flexible intelligent wearable fabrics. © 2024 China Textile Engineering Society. All rights reserved;
D O I：
10.13475/j.fzxb.20240400601
中图分类号：
学科分类号：
摘要：
引用
收藏
页码：1 / 9
相关论文
共 50 条
  • [1] Surface Functionalization Based on Protein Amyloid-like Aggregation
    Fu Chengyu
    Zhou Xingyu
    Yang Peng
    ACTA CHIMICA SINICA, 2023, 81 (11) : 1566 - 1576
  • [2] Amyloid-Like Protein Aggregation Toward Pesticide Reduction
    Su, Hao
    Liu, Yongchun
    Gao, Yingtao
    Fu, Chengyu
    Li, Chen
    Qin, Rongrong
    Liang, Lei
    Yang, Peng
    ADVANCED SCIENCE, 2022, 9 (13)
  • [3] Amyloid-like aggregation of provasopressin
    Spiess, Martin
    Beuret, Nicole
    Baschong, Cristina Prescianotto
    Rutishauser, Jonas
    VASOPRESSIN, 2020, 113 : 55 - 77
  • [4] Synthesis and functionalization of scalable and versatile 2D protein films via amyloid-like aggregation
    Liu, Yongchun
    Miao, Shuting
    Ren, Hao
    Tian, Lihua
    Zhao, Jian
    Yang, Peng
    NATURE PROTOCOLS, 2024, 19 (02) : 539 - 564
  • [5] Synthesis and functionalization of scalable and versatile 2D protein films via amyloid-like aggregation
    Yongchun Liu
    Shuting Miao
    Hao Ren
    Lihua Tian
    Jian Zhao
    Peng Yang
    Nature Protocols, 2024, 19 : 539 - 564
  • [6] Prevention of amyloid-like aggregation as a driving force of protein evolution
    Monsellier, Elodie
    Chiti, Fabrizio
    EMBO REPORTS, 2007, 8 (08) : 737 - 742
  • [7] The biofilm-associated surface protein Esp of Enterococcus faecalis forms amyloid-like fibers
    Agustina Taglialegna
    Leticia Matilla-Cuenca
    Pedro Dorado-Morales
    Susanna Navarro
    Salvador Ventura
    James A. Garnett
    Iñigo Lasa
    Jaione Valle
    npj Biofilms and Microbiomes, 6
  • [8] The biofilm-associated surface protein Esp of Enterococcus faecalis forms amyloid-like fibers
    Taglialegna, Agustina
    Matilla-Cuenca, Leticia
    Dorado-Morales, Pedro
    Navarro, Susanna
    Ventura, Salvador
    Gamete, James A.
    Lasa, Inigo
    Valle, Jaione
    NPJ BIOFILMS AND MICROBIOMES, 2020, 6 (01)
  • [9] Distribution of Amyloid-Like and Oligomeric Species from Protein Aggregation Kinetics
    Silva, Alexandra
    Almeida, Bruno
    Fraga, Joana S.
    Taboada, Pablo
    Martins, Pedro M.
    Macedo-Ribeiro, Sandra
    ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2017, 56 (45) : 14042 - 14045
  • [10] Tuning protein assembly pathways through superfast amyloid-like aggregation
    Li, Chen
    Xu, Lu
    Zuo, Yi Y.
    Yang, Peng
    BIOMATERIALS SCIENCE, 2018, 6 (04) : 836 - 841
12345