Role of peptide self-assembly in antimicrobial peptides

被引:98
|
作者
Tian, Xibo [1 ]
Sun, Fude [1 ]
Zhou, Xi-Rui [1 ]
Luo, Shi-Zhong [1 ]
Chen, Long [1 ]
机构
[1] Beijing Univ Chem Technol, Coll Life Sci & Technol, Beijing Key Lab Bioproc, Beijing 100029, Peoples R China
基金
中国国家自然科学基金;
关键词
antimicrobial peptides; peptide self-assembly; cell selectivity; stability; drug delivery; STATE NMR-SPECTROSCOPY; MOLECULAR-DYNAMICS; CATIONIC PEPTIDES; CELL SELECTIVITY; DESIGNED PEPTIDE; LYTIC PEPTIDE; MEMBRANE; ANTIBACTERIAL; HYDROGELATION; PH;
D O I
10.1002/psc.2788
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Antimicrobial peptides (AMPs) are considered as potential antibiotic substitutes because of their potent activities. Previous studies mainly focused on the effects of peptide charges and secondary structures, but the self-assembly of AMPs was neglected. As more and more researchers notice the roles of peptide self-assembly in AMPs, it has been considered as another important property. In this review, we will discuss the influences of peptide self-assembly on the activity and mode of action, and some specific features it introduces to the AMPs, such as particular responsiveness, improved cell selectivity and stability and sustained release. In addition, some methods to design self-assembling AMPs are primarily discussed. With further understanding about the self-assembling regularity, design of particular self-assembling AMPs will be very helpful for their applications, especially in the fields of drug delivery and biomedical engineering. Copyright (c) 2015 European Peptide Society and John Wiley & Sons, Ltd.
引用
收藏
页码:530 / 539
页数:10
相关论文
共 50 条
  • [31] Biomimetic peptide self-assembly for functional materials
    Levin, Aviad
    Hakala, Tuuli A.
    Schnaider, Lee
    Bernardes, Goncalo J. L.
    Gazit, Ehud
    Knowles, Tuomas P. J.
    NATURE REVIEWS CHEMISTRY, 2020, 4 (11) : 615 - 634
  • [32] Self-assembly of glycerol monooleate with the antimicrobial peptide LL-37: a molecular dynamics study
    Malini, R. Innocenti
    Zabara, M.
    Gontsarik, M.
    Maniura-Weber, K.
    Rossi, R. M.
    Spano, F.
    Salentinig, S.
    RSC ADVANCES, 2020, 10 (14) : 8291 - 8302
  • [33] The Self-Assembly of Helical Peptide Building Blocks
    Mondal, Sudipta
    Gazit, Ehud
    CHEMNANOMAT, 2016, 2 (05): : 323 - 332
  • [34] Self-assembly of amyloid-forming peptides by molecular dynamics simulations
    Wei, Guanghong
    Song, Wei
    Derreumaux, Philippe
    Mousseau, Normand
    FRONTIERS IN BIOSCIENCE-LANDMARK, 2008, 13 : 5681 - 5692
  • [35] Hierarchical self-assembly of Tjernberg peptide at nanoscale
    Kumaraswamy, Priyadharshini
    Sethuraman, Swaminathan
    Krishnan, Uma Maheswari
    SOFT MATTER, 2013, 9 (09) : 2684 - 2694
  • [36] A computational study of the self-assembly of the RFFFR peptide
    Slyngborg, Morten
    Fojan, Peter
    PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 2015, 17 (44) : 30023 - 30036
  • [37] Hierarchical Self-Assembly of Peptides and its Applications in Bionanotechnology
    Gerbelli, Barbara B.
    Vassiliades, Sandra V.
    Rojas, Jose E. U.
    Pelin, Juliane N. B. D.
    Mancini, Rodrigo S. N.
    Pereira, Wallace S. G.
    Aguilar, Andrea M.
    Venanzi, Mariano
    Cavalieri, Francesca
    Giuntini, Francesca
    Alves, Wendel A.
    MACROMOLECULAR CHEMISTRY AND PHYSICS, 2019, 220 (14)
  • [38] Self-assembly of peptides in living cells for disease theranostics
    Mo, Xiaowei
    Zhang, Zeyu
    Song, Jinyan
    Wang, Yushi
    Yu, Zhilin
    JOURNAL OF MATERIALS CHEMISTRY B, 2024, 12 (18) : 4289 - 4306
  • [39] Effect of Solvent on the Self-Assembly of Dialanine and Diphenylalanine Peptides
    Rissanou, Anastassia N.
    Georgilis, Evangelos
    Kasotakis, Emmanouil
    Mitraki, Anna
    Harmandaris, Vagelis
    JOURNAL OF PHYSICAL CHEMISTRY B, 2013, 117 (15) : 3962 - 3975
  • [40] Self-Assembly of Short Amphiphilic Peptides and Their Biomedical Applications
    Le, Xiaosong
    Gao, Tianwen
    Wang, Li
    Wei, Feng
    Chen, Cuixia
    Zhao, Yurong
    CURRENT PHARMACEUTICAL DESIGN, 2022, 28 (44) : 3546 - 3562