Analysis of binding interaction between vitamin B2 and trypsin

Gao, Yan; Zi, Yanqin; Shao, Congying; Wang, Mingru

doi:10.1007/s11164-013-1159-3

Cited by 4 publications

(1 citation statement)

References 16 publications

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“…Gao et al in 2014 demonstrated that riboflavin can interact with trypsin [ 42 ] and Baum et al in 1996 showed that flavins inhibit human cytomegalovirus UL80 protease [ 43 ]. Based on these observations, we have utilized a combination of techniques to evaluate the inhibitory properties of riboflavin against ZIKV and YFV NS2B/NS3 pro and CHIKV nsP2 pro .…”

Section: Introductionmentioning

confidence: 99%

Riboflavin, a Potent Neuroprotective Vitamin: Focus on Flavivirus and Alphavirus Proteases

et al. 2022

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Several neurotropic viruses are members of the flavivirus and alphavirus families. Infections caused by these viruses may cause long-term neurological sequelae in humans. The continuous emergence of infections caused by viruses around the world, such as the chikungunya virus (CHIKV) (Alphavirus genus), the zika virus (ZIKV) and the yellow fever virus (YFV) (both of the Flavivirus genus), warrants the development of new strategies to combat them. Our study demonstrates the inhibitory potential of the water-soluble vitamin riboflavin against NS2B/NS3pro of ZIKV and YFV and nsP2pro of CHIKV. Riboflavin presents a competitive inhibition mode with IC50 values in the medium µM range of 79.4 ± 5.0 µM for ZIKV NS2B/NS3pro and 45.7 ± 2.9 μM for YFV NS2B/NS3pro. Against CHIKV nsP2pro, the vitamin showed a very strong effect (93 ± 5.7 nM). The determined dissociation constants (KD) are significantly below the threshold value of 30 µM. The ligand binding increases the thermal stability between 4 °C and 8 °C. Unexpectedly, riboflavin showed inhibiting activity against another viral protein; the molecule was also able to inhibit the viral entry of CHIKV. Molecular dynamics simulations indicated great stability of riboflavin in the protease active site, which validates the repurposing of riboflavin as a promising molecule in drug development against the viruses presented here.

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Section: Introductionmentioning

confidence: 99%

Riboflavin, a Potent Neuroprotective Vitamin: Focus on Flavivirus and Alphavirus Proteases

et al. 2022

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Fluorescence sensing platform based on ruthenium(II) complexes as high 3S (sensitivity, specificity, speed) and “on-off-on” sensors for the miR-185 detection

Sun

Liang

Xie

et al. 2018

Talanta

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Spectroscopic investigations on the binding of Pyronin Y to human serum albumin

Salcı

Toprak

2016

Journal of Biomolecular Structure and Dynamics

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The interaction of Pyronin Y with human serum albumin (HSA) has been investigated systematically by fluorescence, absorption, fluorescence decay lifetime measurements, FTIR, synchronous fluorescence spectroscopy, and molecular modeling method. The spectroscopic and fluorescence quenching experiments show that Pyronin Y may show a static quenching mechanism with HSA. The specific binding distance of 1.96 nm between HSA and Pyronin Y was obtained via Förster non-radiation energy transfer method. The thermodynamic parameters indicate that the electrostatic interactions play a significant role during the binding process. In addition, synchronous fluorescence and FT-IR spectra indicated that the conformation and microenvironment of HSA were not influenced with the addition of Pyronin Y. The obtained results can be of biological significance in photodynamic therapy.

show abstract

Analysis of binding interaction between vitamin B2 and trypsin

Cited by 4 publications

References 16 publications

Riboflavin, a Potent Neuroprotective Vitamin: Focus on Flavivirus and Alphavirus Proteases

Riboflavin, a Potent Neuroprotective Vitamin: Focus on Flavivirus and Alphavirus Proteases

Fluorescence sensing platform based on ruthenium(II) complexes as high 3S (sensitivity, specificity, speed) and “on-off-on” sensors for the miR-185 detection

Spectroscopic investigations on the binding of Pyronin Y to human serum albumin

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