Arginine-rich self-assembling peptides as potent antibacterial gels

被引:186
|
作者
Veiga, Ana Salome [1 ,2 ]
Sinthuvanich, Chomdao [1 ,3 ]
Gaspar, Diana [2 ]
Franquelim, Henri G. [2 ]
Castanho, Miguel A. R. B. [2 ]
Schneider, Joel P. [1 ]
机构
[1] NCI, Biol Chem Lab, Frederick, MD 21702 USA
[2] Univ Lisbon, Fac Med, Inst Mol Med, P-1649028 Lisbon, Portugal
[3] Univ Delaware, Dept Chem & Biochem, Newark, DE 19716 USA
基金
美国国家卫生研究院;
关键词
Peptide; Self-assembly; Hydrogel; Antibacterial; Syringe delivery; PSEUDOMONAS-AERUGINOSA; ANTIMICROBIAL SURFACES; LIPID-COMPOSITION; EPIDEMIOLOGY; HYDROGEL; DEFENSINS; INFECTIONS; RELEASE;
D O I
10.1016/j.biomaterials.2012.08.046
中图分类号
R318 [生物医学工程];
学科分类号
0831 ;
摘要
Hydrogel materials that display inherent activity against bacteria can be used to directly treat accessible wounds to prevent or kill existing infection. Hydrogels composed of self-assembling beta-hairpin peptides. having a high content of arginine, were found to be extremely effective at killing both gram-positive and gram-negative bacteria, including multi-drug resistant Pseudomonas aeruginosa. No added antibacterial agents are necessary to realize activity. Using self-assembling peptides for material construction allows facile structure-activity relationships to be determined since changes in peptide sequence at the monomer level are directly transposed to the bulk material's antibacterial properties. SAR studies show that arginine content largely influences the hydrogel's antibacterial activity, and influences their bulk rheological properties. These studies culminated in an optimized gel, composed of the peptide PEP6R ((VKVRVRVRVPPTRVRVRVKN)-P-D). PEP6R gels prepared at 1.5 wt % or higher concentration, demonstrate high potency against bacteria, but are cytocompatible toward human erythrocytes as well as mammalian mesenchymal stem cells. Rheological studies indicate that the gel is moderately stiff and displays shear-thin recovery behavior, allowing its delivery via simple syringe. Published by Elsevier Ltd.
引用
收藏
页码:8907 / 8916
页数:10
相关论文
共 50 条
  • [1] Arginine-rich self-assembling peptides form injectable antibacterial hydrogels
    Veiga, A. S.
    Sinthuvanich, C.
    Gaspar, D.
    Franquelim, H. G.
    Castanho, M.
    Schneider, J. P.
    JOURNAL OF PEPTIDE SCIENCE, 2012, 18 : S112 - S112
  • [2] Arginine-rich peptides - Preface
    Futaki, S
    CURRENT PROTEIN & PEPTIDE SCIENCE, 2003, 4 (02)
  • [3] Arginine-rich peptides and their internalization mechanisms
    Futaki, S.
    Nakase, I.
    Taclokoro, A.
    Takeuchi, T.
    Jones, A. T.
    BIOCHEMICAL SOCIETY TRANSACTIONS, 2007, 35 : 784 - 787
  • [4] Stimuli-responsive self-assembling peptides made from antibacterial peptides
    Liu, Yanfei
    Yang, Yanlian
    Wang, Chen
    Zhao, Xiaojun
    NANOSCALE, 2013, 5 (14) : 6413 - 6421
  • [5] Selective Antibacterial Activity and Lipid Membrane Interactions of Arginine-Rich Amphiphilic Peptides
    Edwards-Gayle, Charlotte J. C.
    Barrett, Glyn
    Roy, Shyamali
    Castelletto, Valeria
    Seitsonen, Jani
    Ruokolainen, Janne
    Hamley, Ian W.
    ACS APPLIED BIO MATERIALS, 2020, 3 (02) : 1165 - 1175
  • [6] Self-assembled arginine-rich peptides as effective antimicrobial agents
    Mi, Gujie
    Shi, Di
    Herchek, Whitney
    Webster, Thomas J.
    JOURNAL OF BIOMEDICAL MATERIALS RESEARCH PART A, 2017, 105 (04) : 1046 - 1054
  • [7] Self-assembling amphiphilic peptides
    Dehsorkhi, Ashkan
    Castelletto, Valeria
    Hamley, Ian W.
    JOURNAL OF PEPTIDE SCIENCE, 2014, 20 (07) : 453 - 467
  • [8] Rechargeable antibacterial hydrogels from self-assembling peptides and molecular recognition
    Schneider, Joel
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2019, 258
  • [9] Arginine-rich cell-penetrating peptides
    Schmidt, Nathan
    Mishra, Abhijit
    Lai, Ghee Hwee
    Wong, Gerard C. L.
    FEBS LETTERS, 2010, 584 (09) : 1806 - 1813
  • [10] Micropatterning of bioactive self-assembling gels
    Mata, Alvaro
    Hsu, Lorraine
    Capito, Ramille
    Aparicio, Conrado
    Henrikson, Karl
    Stupp, Samuel I.
    SOFT MATTER, 2009, 5 (06) : 1228 - 1236