Thermosensitive Display of Carbohydrate Ligands on Microgels for Switchable Binding of Proteins and Bacteria

被引:22
|
作者
Paul, Tanja J. [1 ]
Ruebel, Sophie [1 ]
Hildebrandt, Marco [1 ]
Strzelczyk, Alexander K. [1 ]
Spormann, Carina [2 ]
Lindhorst, Thisbe K. [2 ]
Schmidt, Stephan [1 ]
机构
[1] Heinrich Heine Univ Dusseldorf, Inst Organ & Macromol Chem, Univ Str 1, D-40225 Dusseldorf, Germany
[2] Christiana Albertina Univ Kiel, Otto Diels Inst Organ Chem, Otto Hahn Pl 3-4, D-24098 Kiel, Germany
关键词
responsive material; temperature stimulus; LCST; PNIPAM; glycocalyx; lectin; multivalent binding; CELL-ADHESION; TEMPERATURE; SENSITIVITY; PARTICLES;
D O I
10.1021/acsami.9b08537
中图分类号
TB3 [工程材料学];
学科分类号
0805 ; 080502 ;
摘要
The synthesis of carbohydrate-functionalized thermosensitive poly(N-isopropylacrylamide) microgels and their ability to bind carbohydrate-binding pathogens upon temperature switch are reported. It is found that the microgels' binding affinity is increased above their lower critical solution temperature (LCST), enabling thermo-triggerable capture of pathogens. Here, a series of microgels with comparatively low mannose functionalization degrees below 1 mol % is achieved by a single polymerization step. Upon increase in mannose density, the microgel size increases, and the LCST decreases to 26 degrees C. Clustering with concanavalin A indicated that binding affinity is enhanced by a higher mannose content and by raising the temperature above the LCST. Binding studies with Escherichia coli confirm stronger specific interactions above the LCST and formation of mechanically stable aggregates enabling efficient separation of E. coli by filtration. For small incubation times above the LCST, the microgels' potential to release pathogens again below the LCST is confirmed also. Compared to existing switchable scaffolds, microgels nearly entirely composed of a thermosensitive material undergo a large change in volume, which allows them to drastically vary the density of ligands to switch between capture and release. This straightforward yet novel approach is likely compatible with a broad range of bioactive ligands. Therefore, thermosensitive microgels represent a promising platform for the specific capture or release of cells or pathogens.
引用
收藏
页码:26674 / 26683
页数:10
相关论文
共 50 条
  • [21] THE ENERGETICS OF BINDING OF PROTEINS AND LIGANDS TO DNA
    MISRA, VK
    HECHT, J
    HONIG, B
    BIOPHYSICAL JOURNAL, 1993, 64 (02) : A178 - A178
  • [22] ENERGETICS AND DYNAMICS OF BINDING OF LIGANDS TO PROTEINS
    WEBER, G
    ACTA PHARMACEUTICA SUECICA, 1980, 17 (02): : 69 - 69
  • [23] Binding of Ligands to Mitochondrial CISD Proteins
    Napier, Ryan
    Skolik, Robert
    Konkle, Mary
    Menze, Michael
    PROTEIN SCIENCE, 2018, 27 : 63 - 63
  • [24] BINDING OF LIGANDS TO PROTEINS - METHODOLOGICAL APPROACHES
    DIDONATO, A
    ITALIAN JOURNAL OF BIOCHEMISTRY, 1979, 28 (04): : 305 - 306
  • [25] Carbohydrate-binding proteins of marine invertebrates
    P. A. Luk’yanov
    O. V. Chernikov
    S. S. Kobelev
    I. V. Chikalovets
    V. I. Molchanova
    W. Li
    Russian Journal of Bioorganic Chemistry, 2007, 33 : 161 - 169
  • [26] Carbohydrate-binding proteins of marine invertebrates
    Luk'yanov, P. A.
    Chernikov, O. V.
    Kobelev, S. S.
    Chikalovets, I. V.
    Molchanova, V. I.
    Li, W.
    RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY, 2007, 33 (01) : 161 - 169
  • [27] ProCarbDB: a database of carbohydrate-binding proteins
    Copoiu, Liviu
    Torres, Pedro H. M.
    Ascher, David B.
    Blundell, Tom L.
    Malhotra, Sony
    NUCLEIC ACIDS RESEARCH, 2020, 48 (D1) : D368 - D375
  • [28] Computational design of carbohydrate-binding proteins
    Green, David F.
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2011, 241
  • [29] RNA-binding proteins in bacteria
    Holmqvist, Erik
    Vogel, Joerg
    NATURE REVIEWS MICROBIOLOGY, 2018, 16 (10) : 601 - 615
  • [30] IgG-Binding Proteins of Bacteria
    Sidorin, E. V.
    Solov'eva, T. F.
    BIOCHEMISTRY-MOSCOW, 2011, 76 (03) : 295 - 308