Protein Crystallography and Drug Discovery

Rondeau, Jean‐Michel; Schreuder, Herman

doi:10.1016/b978-0-12-417205-0.00022-5

Cited by 8 publications

(6 citation statements)

References 150 publications

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“…X-ray single crystal technique, on the other hand, exploits the fact that X-rays (in the Ångström range, ~10 −8 cm) are scattered (diffracted) by electron cloud of an atom with similar sizes to determine the three dimensional structures of molecules [ 75 ]. Accurate knowledge of molecular structures are known to aid the development of effective drugs [ 76 ] and therapeutic complexes. This is achieved by the growth of crystal, which when diffracted gives useful information such as bond distances, bond angles, and can clearly show the geometry of molecules.…”

Section: Chemistry Of Organotin(iv) Dithiocarbamatementioning

confidence: 99%

Organotin(IV) Dithiocarbamate Complexes: Chemistry and Biological Activity

2018

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Significant attention has been given to organotin(IV) dithiocabamate compounds in recent times. This is due to their ability to stabilize specific stereochemistry in their complexes, and their diverse application in agriculture, biology, catalysis and as single source precursors for tin sulfide nanoparticles. These complexes have good coordination chemistry, stability and diverse molecular structures which, thus, prompt their wide range of biological activities. Their unique stereo-electronic properties underline their relevance in the area of medicinal chemistry. Organotin(IV) dithiocabamate compounds owe their functionalities and usefulness to the individual properties of the organotin(IV) and the dithiocarbamate moieties present within the molecule. These individual properties create a synergy of action in the hybrid complex, prompting an enhanced biological activity. In this review, we discuss the chemistry of organotin(IV) dithiocarbamate complexes that accounts for their relevance in biology and medicine.

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Section: Chemistry Of Organotin(iv) Dithiocarbamatementioning

confidence: 99%

Organotin(IV) Dithiocarbamate Complexes: Chemistry and Biological Activity

2018

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“…X-Ray crystallography has been for decades the most employed biophysical technique for unravelling the structure of lectin–sugar complexes, as atomic resolution information of the complex can be obtained. 26 However, the process of obtaining crystals can be very tedious and the proteins are not always crystallisable. Additionally, due to the intrinsic flexibility of glycans, crystallographic structures usually have erroneous conformations, linkages, or even wrong residues.…”

Section: Introductionmentioning

confidence: 99%

Exploring multivalent carbohydrate–protein interactions by NMR

et al. 2023

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“…9 However, virtual screening based on receptor structure is often dominated by visual inspection of medicinal chemists in the later stage, 10 and many target proteins are still short of a clear and complete crystal structure, which together greatly limit the wide application of the tool. 11 Herein, we reported a multiple-step virtual screening method of receptor structure, based on the homologous modeling of human tyrosinase. Potential active molecules were selected from the compound library constructed by our laboratory for tyrosinase biological activity test.…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Discovery of Tyrosinase Inhibitors: Structure-Based Virtual Screening and Biological Evaluation

Wang

Pan

et al. 2022

Pharmaceutical Fronts

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Tyrosinase (EC 1.14.18.1) plays an indispensable role in the rate-limiting steps of melanin biosynthesis, and its uncontrolled activity may result in various diseases, such as albinism, melanoma, freckles, etc. The inhibition of tyrosinase activity may provide a useful and efficient strategy to treat hyperpigmentation disorders. However, the widely used tyrosinase inhibitors, like α-arbutin, hydroquinone, and kojic acid, have many shortcomings, such as lower efficacy and much more side effects. Herein, we reported the use of homology modeling and multistep structure-based virtual screening for the discovery of novel tyrosinase inhibitors. In this study, 10 initial potential hits (compounds T1–T10) were evaluated for enzyme inhibition and kinetic study, with kojic acid being used as a control. Among them, the IC50 values of both T1 (11.56 ± 0.98 μmol/L) and T5 (18.36 ± 0.82 μmol/L) were superior to that of kojic acid (23.12 ± 1.26 μmol/L). Moreover, T1 and T5 were also identified as the effective noncompetitive tyrosinase inhibitors by the subsequent kinetic study. Above all, T1 and T5 may represent the promising drug candidates for hyperpigmentation therapy in pharmaceutical fields, as well as the effective whitening agents in cosmetic applications.

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Protein Crystallography and Drug Discovery

Cited by 8 publications

References 150 publications

Organotin(IV) Dithiocarbamate Complexes: Chemistry and Biological Activity

Organotin(IV) Dithiocarbamate Complexes: Chemistry and Biological Activity

Exploring multivalent carbohydrate–protein interactions by NMR

Discovery of Tyrosinase Inhibitors: Structure-Based Virtual Screening and Biological Evaluation

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