Chemical Dimerizers in Three-Hybrid Systems for Small Molecule–Target Protein Profiling

2016 ◽  
Vol 11 (8) ◽  
pp. 2075-2090 ◽  
Author(s):  
Dries J. H. De Clercq ◽  
Jan Tavernier ◽  
Sam Lievens ◽  
Serge Van Calenbergh
Keyword(s):  
Hybrid Systems ◽  
Small Molecule ◽  
Protein Profiling ◽  
Target Protein

scholarly journals Colorimetric detection of protein via the terminal protection of small-molecule-linked DNA and unmodified gold nanoparticles

RSC Advances ◽  
2018 ◽  
Vol 8 (68) ◽  
pp. 38758-38764
Author(s):  
Jianwei Zhao ◽  
Cuiping Li ◽  
Guimin Ma ◽  
Wenhui Hao ◽  
Hongxia Jia
Keyword(s):  
Gold Nanoparticles ◽  
Small Molecule ◽  
Colorimetric Detection ◽  
Protein Detection ◽  
Target Protein

A novel colorimetric strategy for protein detection was developed based on unmodified gold nanoparticles (AuNPs) and terminal protection from a target protein.

scholarly journals Small-Molecule Inhibitors That Target Protein-Protein Interactions in the RAD51 Family of Recombinases

ChemMedChem ◽  
2014 ◽  
Vol 10 (2) ◽  
pp. 296-303 ◽  
Author(s):  
Duncan E. Scott ◽  
Anthony G. Coyne ◽  
Ashok Venkitaraman ◽  
Tom L. Blundell ◽  
Chris Abell ◽  
...  
Keyword(s):  
Small Molecule ◽  
Protein Interactions ◽  
Small Molecule Inhibitors ◽  
Target Protein ◽  
Protein Protein Interactions

A GAL4-based yeast three-hybrid system for the identification of small molecule–target protein interactions

2002 ◽  
Vol 63 (9) ◽  
pp. 1619-1628 ◽  
Author(s):  
Debbie C. Henthorn ◽  
Albert A. Jaxa-Chamiec ◽  
Eric Meldrum
Keyword(s):  
Small Molecule ◽  
Hybrid System ◽  
Protein Interactions ◽  
Target Protein

scholarly journals A DNA Electrochemical Sensor via Terminal Protection of Small-Molecule-Linked DNA for Highly Sensitive Protein Detection

Biosensors ◽  
2021 ◽  
Vol 11 (11) ◽  
pp. 451
Author(s):  
Ping Ouyang ◽  
Chenxin Fang ◽  
Jialun Han ◽  
Jingjing Zhang ◽  
Yuxing Yang ◽  
...  
Keyword(s):  
Small Molecule ◽  
Gold Electrode ◽  
Folate Receptor ◽  
Protein Detection ◽  
Disease Diagnosis ◽  
Dna Biosensor ◽  
Target Protein ◽  
Receptor Protein ◽  
Electrochemical Dna Biosensor ◽  
Electrochemical Signal

The qualitative and quantitative determination of marker protein is of great significance in the life sciences and in medicine. Here, we developed an electrochemical DNA biosensor for protein detection based on DNA self-assembly and the terminal protecting effects of small-molecule-linked DNA. This strategy is demonstrated using the small molecule biotin and its receptor protein streptavidin (SA). We immobilized DNA with a designed structure and sequence on the surface of the gold electrode, and we named it M1-Biotin DNA. M1-Biotin DNA selectively combines with SA to generate M1-Biotin-SA DNA and protects M1-Biotin DNA from digestion by EXO III; therefore, M1-Biotin DNA remains intact on the electrode surface. M1-Biotin-SA DNA was modified with methylene blue (MB); the MB reporter molecule is located near the surface of the gold electrode, which generates a substantial electrochemical signal during the detection of SA. Through this strategy, we can exploit the presence or absence of an electrochemical signal to provide qualitative target protein determination as well as the strength of the electrochemical signal to quantitatively analyze the target protein concentration. This strategy has been proven to be used for the quantitative analysis of the interaction between biotin and streptavidin (SA). Under optimal conditions, the detection limit of the proposed biosensor is as low as 18.8 pM, and the linear range is from 0.5 nM to 5 μM, showing high sensitivity. The detection ability of this DNA biosensor in complex serum samples has also been studied. At the same time, we detected the folate receptor (FR) to confirm that this strategy can be used to detect other proteins. Therefore, this electrochemical DNA biosensor provides a sensitive, low-cost, and fast target protein detection platform, which may provide a reliable and powerful tool for early disease diagnosis.

scholarly journals Identification of Target Protein for Bio-active Small Molecule Using Photo-cross Linked Beads and MALDI-TOF Mass Spectrometry

BIO-PROTOCOL ◽  
2020 ◽  
Vol 10 (3) ◽  
Author(s):  
Kruthi Suvarna ◽  
Kaori Honda ◽  
Makoto Muroi ◽  
Yasumitsu Kondoh ◽  
Nobumoto Watanabe ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Small Molecule ◽  
Target Protein ◽  
Maldi Tof Mass Spectrometry ◽  
Maldi Tof

Regenerable Biosensors for Small-Molecule Kinetic Characterization Using SPR

2020 ◽  
pp. 247255522097535
Author(s):  
Anders Gunnarsson ◽  
Christopher J. Stubbs ◽  
Philip B. Rawlins ◽  
Eleanor Taylor-Newman ◽  
Wei-chao Lee ◽  
...  
Keyword(s):  
Small Molecule ◽  
Kinase Inhibitors ◽  
Covalent Immobilization ◽  
Target Protein ◽  
Kinetic Characterization ◽  
Dissociation Kinetics ◽  
Baseline Drift ◽  
Reversible Immobilization ◽  
Immobilization Techniques

A key activity in small-molecule drug discovery is the characterization of compound–target interactions. Surface plasmon resonance (SPR) is a flexible technique for this purpose, with a wide affinity range (micromoles to picomoles), low protein requirements, and the ability to characterize the kinetics of compound binding. However, a key requirement of SPR is the immobilization of the target protein to the surface of the sensor chip. The most commonly used immobilization techniques (covalent immobilization, streptavidin–biotin) are irreversible in nature, which can afford excellent baseline stability but impose limitations throughput for slowly dissociating compounds or unstable targets. Reversible immobilization (e.g., His-tag–Ni-NTA) is possible but typically precludes accurate quantification of slow dissociation kinetics due to baseline drift. Here we present our investigation of three immobilization strategies (dual-His-tagged target protein, His-tagged streptavidin, and switchavidin) that combine the robustness of irreversible immobilization with the flexibility of reversible immobilization. Each has its own advantages and limitations, and while a universal immobilization procedure remains to be found, these strategies add to the immobilization toolbox that enables previously out-of-scope applications. Such applications are highlighted in two examples that greatly increased throughput for the kinetic characterization of potent kinase inhibitors and kinetic profiling of covalent inhibitors.

scholarly journals Discovery of small-molecule enzyme activators by activity-based protein profiling

2020 ◽  
Vol 16 (9) ◽  
pp. 997-1005 ◽  
Author(s):  
Bernard P. Kok ◽  
Srijana Ghimire ◽  
Woojoo Kim ◽  
Shreyosree Chatterjee ◽  
Tyler Johns ◽  
...  
Keyword(s):  
Small Molecule ◽  
Protein Profiling ◽  
Enzyme Activators
Sign in / Sign up

Export Citation Format

Share Document