Site-Specific Functionalization of Hyperbranched Polymers Using “Click” Chemistry

2009 ◽  
Vol 42 (12) ◽  
pp. 4028-4037 ◽  
Author(s):  
Animesh Saha ◽  
S. Ramakrishnan
Keyword(s):  
Click Chemistry ◽  
Hyperbranched Polymers ◽  
Site Specific

A modified dinucleotide for site-specific RNA-labelling by transcription priming and click chemistry

2014 ◽  
Vol 50 (11) ◽  
pp. 1313-1316 ◽  
Author(s):  
Ayan Samanta ◽  
André Krause ◽  
Andres Jäschke
Keyword(s):  
Click Chemistry ◽  
Site Specific

Site-Specific Surface Functionalization via Microchannel Cantilever Spotting (µCS): Comparison between Azide-Alkyne and Thiol-Alkyne Click Chemistry Reactions

Small ◽  
2018 ◽  
Vol 14 (21) ◽  
pp. 1800131 ◽  
Author(s):  
Seyed Mohammad Mahdi Dadfar ◽  
Sylwia Sekula-Neuner ◽  
Uwe Bog ◽  
Vanessa Trouillet ◽  
Michael Hirtz
Keyword(s):  
Specific Surface ◽  
Click Chemistry ◽  
Surface Functionalization ◽  
Site Specific

scholarly journals Grafting Hyperbranched Polymers onto TiO2 Nanoparticles via Thiol-yne Click Chemistry and Its Effect on the Mechanical, Thermal and Surface Properties of Polyurethane Coating

Materials ◽  
2019 ◽  
Vol 12 (17) ◽  
pp. 2817 ◽  
Author(s):  
Feng Zhan ◽  
Lei Xiong ◽  
Fang Liu ◽  
Chenying Li
Keyword(s):  
Click Chemistry ◽  
Tio2 Nanoparticles ◽  
Photoelectron Spectroscopy ◽  
Hyperbranched Polymers ◽  
Nanocomposite Coatings ◽  
Mechanical And Thermal Properties ◽  
Nanoparticle Dispersion ◽  
X Ray Diffraction ◽  
X Ray ◽  
Surface Modified

In this study, we proposed a novel and facile method to modify the surface of TiO2 nanoparticles and investigated the influence of the surface-modified TiO2 nanoparticles as an additive in a polyurethane (PU) coating. The hyperbranched polymers (HBP) were grafted on the surface of TiO2 nanoparticles via the thiol-yne click chemistry to reduce the aggregation of nanoparticles and increase the interaction between TiO2 and polymer matrices. The grafting of HBP on the TiO2 nanoparticles surface was investigated by means of X-ray photoelectron spectroscopy (XPS), X-ray diffraction (XRD), Fourier transform infrared (FT-IR), nuclear magnetic resonance (NMR) and thermogravimetry analysis (TGA). The thermal and mechanical properties of nanocomposite coatings containing various amounts of TiO2 nanoparticles were measured by dynamic mechanical thermal (DMTA) and tensile strength measurement. Moreover, the surface structure and properties of the newly prepared nanocomposite coatings were examined. The experimental results demonstrate that the incorporation of the surface-modified TiO2 nanoparticles can improve the mechanical and thermal properties of nanocomposite coatings. The results also reveal that the surface modification of TiO2 with the HBP chains improves the nanoparticle dispersion, and the coating surface shows a lotus leaf-like microstructure. Thus, the functional nanocomposite coatings exhibit superhydrophobic properties, good photocatalytic depollution performance, and high stripping resistance.

Polymer Pen Lithography (PPL)-Induced Site-Specific Click Chemistry for the Formation of Functional Glycan Arrays

Small ◽  
2012 ◽  
Vol 8 (13) ◽  
pp. 2000-2005 ◽  
Author(s):  
Shudan Bian ◽  
Jiajun He ◽  
Kevin B. Schesing ◽  
Adam B. Braunschweig
Keyword(s):  
Click Chemistry ◽  
Site Specific ◽  
Polymer Pen Lithography

scholarly journals Site‐specific Bioconjugation and Convergent Click Chemistry Enhances Antibody–Chromophore Conjugate Binding Efficiency

2020 ◽  
Vol 96 (3) ◽  
pp. 596-603 ◽  
Author(s):  
Amissi Sadiki ◽  
Eric M. Kercher ◽  
Haibin Lu ◽  
Ryan T. Lang ◽  
Bryan Q. Spring ◽  
...  
Keyword(s):  
Click Chemistry ◽  
Site Specific

scholarly journals Antibiotic Spider Silk: Site-Specific Functionalization of Recombinant Spider Silk Using “Click” Chemistry

2016 ◽  
Vol 29 (10) ◽  
pp. 1604245 ◽  
Author(s):  
David Harvey ◽  
Philip Bardelang ◽  
Sara L. Goodacre ◽  
Alan Cockayne ◽  
Neil R. Thomas
Keyword(s):  
Click Chemistry ◽  
Spider Silk ◽  
Site Specific

scholarly journals Aqueous synthesis of a small-molecule lanthanide chelator amenable to copper-free click chemistry

2019 ◽  
Author(s):  
Stephanie Cara Bishop ◽  
Robert Winefield ◽  
Asokan Anbanandam ◽  
Jed Noah Lampe
Keyword(s):  
Click Chemistry ◽  
Small Molecule ◽  
Unnatural Amino Acids ◽  
Protein Denaturation ◽  
Copper Catalyst ◽  
Chelating Agent ◽  
Unnatural Amino Acid ◽  
Aqueous Synthesis ◽  
Site Specific ◽  
Biophysical Studies

The lanthanides (Ln3+), or rare earth elements, have proven to be useful tools for biomolecular NMR, X-ray crystallographic, and fluorescence analyses due to their unique 4f orbitals. However, their utility in biological applications has been limited because site-specific incorporation of a chelating element is required to ensure efficient binding of the free Ln3+ ion. Additionally, current Ln3+ chelator syntheses complicate efforts to directly incorporate Ln3+ chelators into proteins as the multi-step processes and a reliance on organic solvents promote protein denaturation and aggregation which are generally incompatible with direct incorporation into the protein of interest. To overcome these limitations, herein we describe a two-step aqueous synthesis of a small molecule lanthanide chelating agent amenable to site-specific incorporation into a protein using copper-free click chemistry with unnatural amino acids. The bioconjugate combines a diethylenetriaminepentaacetic acid (DTPA) chelating moiety with a clickable dibenzylcyclooctyne-amine (DBCO-amine) to facilitate the reaction with an azide containing unnatural amino acid. Incorporating the DBCO-amine avoids the use of the cytotoxic Cu2+ ion as a catalyst. The clickable lanthanide chelator (CLC) reagent reacted readily with p-azidophenylalanine (paF) without the need of a copper catalyst, thereby demonstrating proof-of-concept. Implementation of the orthogonal click chemistry reaction has the added advantage that the chelator can be used directly in a protein labeling reaction, without the need of extensive purification. Given the inherent advantages of Cu2+-free click chemistry, aqueous synthesis, and facile labeling, we believe that the CLC will find abundant use in both structural and biophysical studies of proteins and their complexes.

scholarly journals Enzyme-Mediated Methodology for the Site-Specific Radiolabeling of Antibodies Based on Catalyst-Free Click Chemistry

2013 ◽  
Vol 24 (6) ◽  
pp. 1057-1067 ◽  
Author(s):  
Brian M. Zeglis ◽  
Charles B. Davis ◽  
Robert Aggeler ◽  
Hee Chol Kang ◽  
Aimei Chen ◽  
...  
Keyword(s):  
Click Chemistry ◽  
Site Specific ◽  
Catalyst Free
Sign in / Sign up

Export Citation Format

Share Document