Sensing Capabilities of Colloidal Gold Monolayer Modified with a Phenylboronic Acid-Carrying Polymer Brush

2006 ◽  
Vol 7 (4) ◽  
pp. 1065-1071 ◽  
Author(s):  
Hiromi Kitano ◽  
Yasutaka Anraku ◽  
Hiroaki Shinohara
Keyword(s):  
Colloidal Gold ◽  
Phenylboronic Acid ◽  
Polymer Brush

Binding of Ricinus communis agglutinin to a galactose-carrying polymer brush on a colloidal gold monolayer

2008 ◽  
Vol 66 (1) ◽  
pp. 110-118 ◽  
Author(s):  
Kazuya Mizukami ◽  
Hajime Takakura ◽  
Takayuki Matsunaga ◽  
Hiromi Kitano
Keyword(s):  
Colloidal Gold ◽  
Ricinus Communis ◽  
Polymer Brush ◽  
Ricinus Communis Agglutinin

Dual-Responsive Surfaces Modified with Phenylboronic Acid-Containing Polymer Brush To Reversibly Capture and Release Cancer Cells

2013 ◽  
Vol 135 (20) ◽  
pp. 7603-7609 ◽  
Author(s):  
Hongliang Liu ◽  
Yingying Li ◽  
Kang Sun ◽  
Junbing Fan ◽  
Pengchao Zhang ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Phenylboronic Acid ◽  
Polymer Brush ◽  
Dual Responsive ◽  
Responsive Surfaces ◽  
Capture And Release

Colloidal Gold Nanoparticles as Catalyst for Carbon−Carbon Bond Formation:  Application to Aerobic Homocoupling of Phenylboronic Acid in Water

Langmuir ◽  
2004 ◽  
Vol 20 (26) ◽  
pp. 11293-11296 ◽  
Author(s):  
Hironori Tsunoyama ◽  
Hidehiro Sakurai ◽  
Nobuyuki Ichikuni ◽  
Yuichi Negishi ◽  
Tatsuya Tsukuda
Keyword(s):  
Gold Nanoparticles ◽  
Colloidal Gold ◽  
Phenylboronic Acid ◽  
Bond Formation ◽  
Carbon Bond ◽  
Colloidal Gold Nanoparticles ◽  
Carbon Carbon Bond

Temperature-responsive polymer brush constructed on a colloidal gold monolayer

2009 ◽  
Vol 331 (2) ◽  
pp. 343-350 ◽  
Author(s):  
Hiromi Kitano ◽  
Hirokazu Kago ◽  
Kazuhiro Matsuura
Keyword(s):  
Colloidal Gold ◽  
Polymer Brush ◽  
Temperature Responsive ◽  
Responsive Polymer

scholarly journals Phenylboronic acid modification augments the lysosome escape and antitumor efficacy of a cylindrical polymer brush-based prodrug

2021 ◽  
Author(s):  
Ruonan Wang ◽  
Changfeng Yin ◽  
Changren Liu ◽  
Ying Sun ◽  
Panpan Xiao ◽  
...  
Keyword(s):  
Polymer Brushes ◽  
Drug Loading ◽  
Phenylboronic Acid ◽  
Polymer Brush ◽  
Specific Interactions ◽  
Acid Modification ◽  
Tumor Penetration ◽  
Lysosomal Membrane Proteins ◽  
Shock Proteins ◽  
First Time

Abstract Timely lysosome escape is very important for nanomedicines to avoid premature degradation. Herein, we report an exciting finding that phenylboronic acid (PBA) modification can greatly facilitate the lysosome escape of cylindrical polymer brushes (CPBs), and further promote their exocytosis and transcellular transfer. This fundamental finding for the first time reveals that PBA groups improve the tumor penetration of nanomaterials via an active transcytosis mechanism. We speculate that the mechanism of the PBA-enhanced lysosome escape is associated with the specific interactions of the PBA group with the lysosomal membrane proteins and hot shock proteins. The featured advantage of the PBA modification over the known lysosome escape strategies is that it does not cause significant adverse effects on the properties of the CPBs. Furthermore, doxorubicin was conjugated to the PBA-modified CPBs with drug loading content larger than 20%. This CPBs-based prodrug could eradicate the tumors established in mice by multiple intravenous administration.

Efficient enrichment of glycopeptides using phenylboronic acid polymer brush modified silica microspheres

2014 ◽  
Vol 2 (16) ◽  
pp. 2276-2281 ◽  
Author(s):  
Xiuling Li ◽  
Hongliang Liu ◽  
Guangyan Qing ◽  
Shutao Wang ◽  
Xinmiao Liang
Keyword(s):  
Synergistic Effect ◽  
High Selectivity ◽  
Phenylboronic Acid ◽  
Polymer Brush ◽  
Hydrogen Binding ◽  
Silica Microspheres ◽  
Modified Silica ◽  
Hydrophilic Nature

Phenylboronic acid (PBA) polymer brush modified silica demonstrated high selectivity for glycopeptides attributed to the synergistic effect of polyvalent interactions, hydrogen binding and hydrophilic nature provided by the polymer brush.

3-D organization of fibrinogen receptors using computer reconstruction and whole-mount microscopy

1988 ◽  
Vol 46 ◽  
pp. 30-31
Author(s):  
E. T. O'Toole ◽  
R. R. Hantgan ◽  
J. C. Lewis
Keyword(s):  
Whole Blood ◽  
Colloidal Gold ◽  
Blood Platelets ◽  
Cell Contact ◽  
Computer Assisted ◽  
Adherent Cells ◽  
Differential Centrifugation ◽  
Computer Reconstruction ◽  
Sds Page ◽  
Whole Mount

Thrombocytes (TC), the avian equivalent of blood platelets, support hemostasis by aggregating at sites of injury. Studies in our lab suggested that fibrinogen (fib) is a requisite cofactor for TC aggregation but operates by an undefined mechanism. To study the interaction of fib with TC and to identify fib receptors on cells, fib was purified from pigeon plasma, conjugated to colloidal gold and used both to facilitate aggregation and as a receptor probe. Described is the application of computer assisted reconstruction and stereo whole mount microscopy to visualize the 3-D organization of fib receptors at sites of cell contact in TC aggregates and on adherent cells.Pigeon TC were obtained from citrated whole blood by differential centrifugation, washed with Ca++ free Hank's balanced salts containing 0.3% EDTA (pH 6.5) and resuspended in Ca++ free Hank's. Pigeon fib was isolated by precipitation with PEG-1000 and the purity assessed by SDS-PAGE. Fib was conjugated to 25nm colloidal gold by vortexing and the conjugates used as the ligand to identify fib receptors.

The Application of Protein A-Gold Immunocytochemistry to Studies of Protein Secretion

1985 ◽  
Vol 43 ◽  
pp. 426-429
Author(s):  
George H. Herbener ◽  
Antonio Nanci ◽  
Moise Bendayan
Keyword(s):  
Tissue Section ◽  
Colloidal Gold ◽  
Unit Area ◽  
Protein A ◽  
Extracellular Proteins ◽  
Gold Complex ◽  
Second Step ◽  
Igg Antibodies ◽  
Tissue Sections ◽  
Antigenic Sites

Protein A-gold immunocytochemistry is a two-step, post-embedding labeling procedure which may be applied to tissue sections to localize intra- and extracellular proteins. The key requisite for immunocytochemistry is the availability of the appropriate antibody to react in an immune response with the antigenic sites on the protein of interest. During the second step, protein A-gold complex is reacted with the antibody. This is a non- specific reaction in that protein A will combine with most IgG antibodies. The ‘label’ visualized in the electron microscope is colloidal gold. Since labeling is restricted to the surface of the tissue section and since colloidal gold is particulate, labeling density, i.e., the number of gold particles per unit area of tissue section, may be quantitated with ease and accuracy.

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