Chiral separation of new sulfonamide derivatives and evaluation of their enantioselective affinity for human carbonic anhydrase II by microscale thermophoresis and surface plasmon resonance

Rogez-Florent, Tiphaine; Foulon, Catherine; Drucbert, Anne-Sophie; Schifano, Nadège; Six, Perrine; Devassine, Stéphanie; Depreux, Patrick; Danzé, Pierre‐Marie; Goossens, Laurence; Danel, Cécile; Goossens, Jean‐François

doi:10.1016/j.jpba.2017.01.023

Cited by 18 publications

(10 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A normalized MST time trajectory was obtained at 20 s. The regular shape of the curve indicated that no dimer aggregation occurred. 30 Compared with WT AK, K d of M372I/T379W AK for the substrate Asp decreased (from 655.08 to 482.64 mM; Fig. 4A and B), indicating that the binding affinity of AK for the substrate Asp signicantly strengthened aer the mutations.…”

Section: Specic Binding Of Ak To the Substrate Asp And Inhibitor Lysmentioning

confidence: 94%

“…The optimum temperature of the enzyme was determined by incubation of the reaction mixture (the enzymatic-activity assay system) at 15,20,25,26,28,30,35,40,45, or 50 C. The optimum pH of the enzyme was determined using 100 mM Tris-HCl with adjustment of buffer pH from 6 to 10 in 0.5-unit steps. The maximum enzymatic activity, which was achieved at the optimum temperature and pH, was set to 100%.…”

Section: Ak Activity and Steady-state Kinetics Assaysmentioning

confidence: 99%

“…Longer the half-life, better the stability of the enzyme. The AK puried solution was incubated at 20,28,30,35,40, and 45 C (pH 7.4) for 1-10 h, respectively. Enzyme activity was assayed every 1 h, as described previously.…”

Section: Thermostability Of the Wild-type And Mutant Aksmentioning

confidence: 99%

See 2 more Smart Citations

Enzymatic characterization and molecular mechanism of a novel aspartokinase mutant M372I/T379W fromCorynebacterium pekinense

Gao

Han

et al. 2019

RSC Adv.

View full text Add to dashboard Cite

show abstract

Section: Specic Binding Of Ak To the Substrate Asp And Inhibitor Lysmentioning

confidence: 94%

Section: Ak Activity and Steady-state Kinetics Assaysmentioning

confidence: 99%

See 1 more Smart Citation

Enzymatic characterization and molecular mechanism of a novel aspartokinase mutant M372I/T379W fromCorynebacterium pekinense

Gao

Han

et al. 2019

RSC Adv.

View full text Add to dashboard Cite

show abstract

“…There are several applications for using of MST in measuring small molecules affinity to proteins for therapeutic and technological developments. Drug discovery is the mainstream of different experimental approaches in protein-small molecule interactions, and a large number of studies are consistent with this general aim [51][52][53][54][55][56][57]. For instance, Patniak et al [58] investigated the affinity of candidate small lead compounds to glucocerebrosidase enzymes (GCase).…”

Section: Protein-small Molecule Interactionmentioning

confidence: 98%

“…MST approaches were carried out after high throughput screening for a huge number of lead compounds to identify series of compounds that activate GCase, which is considered a good target drug for treatment of Gaucher disease. Moreover, Rogez-Florent et al [57] investigated the enantioselective affinity of new sulfonamide derivatives to human carbonic anhydrase enzymes. In this substantial approach, MST and SPR were used for the interaction study.…”

Section: Protein-small Molecule Interactionmentioning

confidence: 99%

Thermophoresis for characterizing biomolecular interaction

Asmari

Ratih

Alhazmi

et al. 2018

Methods

View full text Add to dashboard Cite

The study of biomolecular interactions is crucial to get more insight into the biological system. The interactions of protein-protein, protein-nucleic acids, protein-sugars, nucleic acid-nucleic acids and protein-small molecules are supporting therapeutics and technological developments. Recently, the development in a large number of analytical techniques for characterizing biomolecular interactions reflect the promising research investments in this field. In this review, microscale thermophoresis technology (MST) is presented as an analytical technique for characterizing biomolecular interactions. Recent years have seen much progress and several applications established. MST is a powerful technique in quantitation of binding events based on the movement of molecules in microscopic temperature gradient. Simplicity, free solutions analysis, low sample volume, short analysis time, and immobilization free are the MST advantages over other competitive techniques. A wide range of studies in biomolecular interactions have been successfully carried out using MST, which tend to the versatility of the technique to use in screening binding events in order to save time, cost and obtained high data quality.

show abstract

Thermophoretic Assay for Biosensing

Ling,

Yuan,

Chen

et al. 2024

Adv Materials Technologies

View full text Add to dashboard Cite

Thermophoresis refers to the directional movement of particles driven by temperature gradients, which is ubiquitous in nature. This phenomenon can be conveniently used to manipulate molecules and objects such as biomolecules, colloids, metal nanoparticles, and cells. Because of these advantages, thermophoresis is widely used in biosensing. In vitro diagnosis, as an important field of biosensing, is highly compatible with thermophoresis. Compared with traditional in vitro diagnostic techniques, thermophoretic diagnosis is a homogeneous system that boasts high efficiency and rapid detection as well as a wide detection range; thus, thermophoresis has a myriad of applications. The emergence of microscale and multifield coupling thermophoresis technologies yield widespread applications of thermophoresis in the field of in vitro diagnostics. This study presents the history of thermophoresis and reviews various cases of biosensors utilizing thermophoresis. Those biosensors are widely used in in vitro diagnostics, biomarker discovery, and other fields. Furthermore, it assesses the advantages of thermophoresis, and finally discusses its current challenges and future development.

show abstract

Chiral separation of new sulfonamide derivatives and evaluation of their enantioselective affinity for human carbonic anhydrase II by microscale thermophoresis and surface plasmon resonance

Cited by 18 publications

References 29 publications

Enzymatic characterization and molecular mechanism of a novel aspartokinase mutant M372I/T379W fromCorynebacterium pekinense

Enzymatic characterization and molecular mechanism of a novel aspartokinase mutant M372I/T379W fromCorynebacterium pekinense

Thermophoresis for characterizing biomolecular interaction

Thermophoretic Assay for Biosensing

Contact Info

Product

Resources

About