Complex formation of rutin and quercetin with copper alters the mode of inhibition of Ribonuclease A

Debi Ranjan Tripathy; Atanu Singha Roy; Swagata Dasgupta

doi:10.1016/j.febslet.2011.09.005

Complex formation of rutin and quercetin with copper alters the mode of inhibition of Ribonuclease A

Debi Ranjan Tripathy, Atanu Singha Roy, Swagata Dasgupta^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

Abstract

Rutin and quercetin, both minor components of green tea and their Cu(II) complexes interact with Ribonuclease A (RNase A) in a novel way. The effects of rutin, quercetin and their copper complexes on the catalytic activity of the protein were investigated. Rutin shows an enhancement in the ribonucleolytic activity whereas the copper complexes and quercetin behave as non-competitive type inhibitors with K _i values in the μM range. The secondary structural changes of RNase A in presence of the ligands were measured by circular dichroism and Fourier transform infrared spectroscopy. The binding parameters were obtained using a fluorescence quenching analysis.

Original language	English
Pages (from-to)	3270-3276
Number of pages	7
Journal	FEBS Letters
Volume	585
Issue number	20
DOIs	https://doi.org/10.1016/j.febslet.2011.09.005
State	Published - 20 Oct 2011
Externally published	Yes

Keywords

Copper complexes
Inhibition
Quercetin
Ribonuclease A
Rutin

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10.1016/j.febslet.2011.09.005

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title = "Complex formation of rutin and quercetin with copper alters the mode of inhibition of Ribonuclease A",

abstract = "Rutin and quercetin, both minor components of green tea and their Cu(II) complexes interact with Ribonuclease A (RNase A) in a novel way. The effects of rutin, quercetin and their copper complexes on the catalytic activity of the protein were investigated. Rutin shows an enhancement in the ribonucleolytic activity whereas the copper complexes and quercetin behave as non-competitive type inhibitors with K i values in the μM range. The secondary structural changes of RNase A in presence of the ligands were measured by circular dichroism and Fourier transform infrared spectroscopy. The binding parameters were obtained using a fluorescence quenching analysis.",

keywords = "Copper complexes, Inhibition, Quercetin, Ribonuclease A, Rutin",

author = "Tripathy, {Debi Ranjan} and {Singha Roy}, Atanu and Swagata Dasgupta",

note = "Funding Information: SDG is grateful to Council of Scientific and Industrial Research (CSIR), India for financial support for the project [01(2115)/07/EMR-II] and CRF, IIT Kharagpur for instrumental facilities D.R.T. and A.S.R. thank CSIR, New Delhi for fellowships. ",

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doi = "10.1016/j.febslet.2011.09.005",

language = "אנגלית",

volume = "585",

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journal = "FEBS Letters",

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AU - Tripathy, Debi Ranjan

AU - Singha Roy, Atanu

AU - Dasgupta, Swagata

N1 - Funding Information: SDG is grateful to Council of Scientific and Industrial Research (CSIR), India for financial support for the project [01(2115)/07/EMR-II] and CRF, IIT Kharagpur for instrumental facilities D.R.T. and A.S.R. thank CSIR, New Delhi for fellowships.

PY - 2011/10/20

Y1 - 2011/10/20

N2 - Rutin and quercetin, both minor components of green tea and their Cu(II) complexes interact with Ribonuclease A (RNase A) in a novel way. The effects of rutin, quercetin and their copper complexes on the catalytic activity of the protein were investigated. Rutin shows an enhancement in the ribonucleolytic activity whereas the copper complexes and quercetin behave as non-competitive type inhibitors with K i values in the μM range. The secondary structural changes of RNase A in presence of the ligands were measured by circular dichroism and Fourier transform infrared spectroscopy. The binding parameters were obtained using a fluorescence quenching analysis.

AB - Rutin and quercetin, both minor components of green tea and their Cu(II) complexes interact with Ribonuclease A (RNase A) in a novel way. The effects of rutin, quercetin and their copper complexes on the catalytic activity of the protein were investigated. Rutin shows an enhancement in the ribonucleolytic activity whereas the copper complexes and quercetin behave as non-competitive type inhibitors with K i values in the μM range. The secondary structural changes of RNase A in presence of the ligands were measured by circular dichroism and Fourier transform infrared spectroscopy. The binding parameters were obtained using a fluorescence quenching analysis.

KW - Copper complexes

KW - Inhibition

KW - Quercetin

KW - Ribonuclease A

KW - Rutin

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JO - FEBS Letters

JF - FEBS Letters

IS - 20

ER -

Complex formation of rutin and quercetin with copper alters the mode of inhibition of Ribonuclease A

Abstract

Keywords

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