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Noncovalent Interaction of Lactoferrin with Epicatechin and Epigallocatechin: Focus on Fluorescence Quenching and Antioxidant Properties
[Image: see text] Lactoferrin (LF) from bovine milk possesses antioxidant activity, immune regulatory and other biological activities. However, the effects of epicatechin (EC) and epigallocatechin (EGC) interacting with LF on the antioxidant activity of LF have not been investigated. Therefore, this...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10633880/ https://www.ncbi.nlm.nih.gov/pubmed/37970015 http://dx.doi.org/10.1021/acsomega.3c06560 |
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author | Chen, Junliang Ma, Shuhua Chen, Xin Dai, Xin Zhang, Li Yuan, Yunxia Li, Linlin Zhang, Hui Liu, Gangtian Ren, Guangyue Duan, Xu Xie, Qinggang Cao, Weiwei |
author_facet | Chen, Junliang Ma, Shuhua Chen, Xin Dai, Xin Zhang, Li Yuan, Yunxia Li, Linlin Zhang, Hui Liu, Gangtian Ren, Guangyue Duan, Xu Xie, Qinggang Cao, Weiwei |
author_sort | Chen, Junliang |
collection | PubMed |
description | [Image: see text] Lactoferrin (LF) from bovine milk possesses antioxidant activity, immune regulatory and other biological activities. However, the effects of epicatechin (EC) and epigallocatechin (EGC) interacting with LF on the antioxidant activity of LF have not been investigated. Therefore, this study aimed to explore their interaction mechanism and the antioxidant activity of LF. UV spectra revealed that EGC (100 μM) induced a higher blue shift of LF at the maximum absorption wavelength than that of EC (100 μM). Fluorescence spectra results suggested that LF fluorescence was quenched by EC and EGC in the static type, which changed the polarity of the microenvironment around LF. The quenching constants K(sv) (5.91 × 10(3)–9.20 × 10(3)) of EC-LF complexes at different temperatures were all higher than that (1.35 × 10(3)–1.75 × 10(3)) of the EGC-LF complex. EC could bind to LF via hydrophobic interactions while hydrogen bonding and van der Waals forces drove the binding of EGC to LF. Both the EC-LF complex and EGC-LF complex could bind to LF with one site. EGC formed more hydrogen bonds with LF than that of EC. The antioxidant activity of LF was increased by the high addition level of EC and EGC. These findings would provide more references for developing LF-catechin complexes as functional antioxidants. |
format | Online Article Text |
id | pubmed-10633880 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-106338802023-11-15 Noncovalent Interaction of Lactoferrin with Epicatechin and Epigallocatechin: Focus on Fluorescence Quenching and Antioxidant Properties Chen, Junliang Ma, Shuhua Chen, Xin Dai, Xin Zhang, Li Yuan, Yunxia Li, Linlin Zhang, Hui Liu, Gangtian Ren, Guangyue Duan, Xu Xie, Qinggang Cao, Weiwei ACS Omega [Image: see text] Lactoferrin (LF) from bovine milk possesses antioxidant activity, immune regulatory and other biological activities. However, the effects of epicatechin (EC) and epigallocatechin (EGC) interacting with LF on the antioxidant activity of LF have not been investigated. Therefore, this study aimed to explore their interaction mechanism and the antioxidant activity of LF. UV spectra revealed that EGC (100 μM) induced a higher blue shift of LF at the maximum absorption wavelength than that of EC (100 μM). Fluorescence spectra results suggested that LF fluorescence was quenched by EC and EGC in the static type, which changed the polarity of the microenvironment around LF. The quenching constants K(sv) (5.91 × 10(3)–9.20 × 10(3)) of EC-LF complexes at different temperatures were all higher than that (1.35 × 10(3)–1.75 × 10(3)) of the EGC-LF complex. EC could bind to LF via hydrophobic interactions while hydrogen bonding and van der Waals forces drove the binding of EGC to LF. Both the EC-LF complex and EGC-LF complex could bind to LF with one site. EGC formed more hydrogen bonds with LF than that of EC. The antioxidant activity of LF was increased by the high addition level of EC and EGC. These findings would provide more references for developing LF-catechin complexes as functional antioxidants. American Chemical Society 2023-10-25 /pmc/articles/PMC10633880/ /pubmed/37970015 http://dx.doi.org/10.1021/acsomega.3c06560 Text en © 2023 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Chen, Junliang Ma, Shuhua Chen, Xin Dai, Xin Zhang, Li Yuan, Yunxia Li, Linlin Zhang, Hui Liu, Gangtian Ren, Guangyue Duan, Xu Xie, Qinggang Cao, Weiwei Noncovalent Interaction of Lactoferrin with Epicatechin and Epigallocatechin: Focus on Fluorescence Quenching and Antioxidant Properties |
title | Noncovalent Interaction
of Lactoferrin with Epicatechin
and Epigallocatechin: Focus on Fluorescence Quenching and Antioxidant
Properties |
title_full | Noncovalent Interaction
of Lactoferrin with Epicatechin
and Epigallocatechin: Focus on Fluorescence Quenching and Antioxidant
Properties |
title_fullStr | Noncovalent Interaction
of Lactoferrin with Epicatechin
and Epigallocatechin: Focus on Fluorescence Quenching and Antioxidant
Properties |
title_full_unstemmed | Noncovalent Interaction
of Lactoferrin with Epicatechin
and Epigallocatechin: Focus on Fluorescence Quenching and Antioxidant
Properties |
title_short | Noncovalent Interaction
of Lactoferrin with Epicatechin
and Epigallocatechin: Focus on Fluorescence Quenching and Antioxidant
Properties |
title_sort | noncovalent interaction
of lactoferrin with epicatechin
and epigallocatechin: focus on fluorescence quenching and antioxidant
properties |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10633880/ https://www.ncbi.nlm.nih.gov/pubmed/37970015 http://dx.doi.org/10.1021/acsomega.3c06560 |
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