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山奈酚-乳铁蛋白复合物的结构及体外抗癌特性

Structural and in vitro anticancer properties of the kaempferol-lactoferrin complex.

作者信息

Xue Peiyu, Zhao Hongmei, You Xinyong, Yue Weiming

机构信息

School of Biology and Food Engineering Anyang Institute of Technology Anyang China.

Department of Thoracic Surgery Qilu Hospital of Shandong University Jinan China.

出版信息

Food Sci Nutr. 2024 Sep 19;12(11):9046-9055. doi: 10.1002/fsn3.4479. eCollection 2024 Nov.

DOI:10.1002/fsn3.4479
PMID:39620007
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11606874/
Abstract

Lactoferrin and polyphenols are common natural functional compounds. Their interactions and the consequential alterations in functional activity have received widespread attention. The work aimed to investigate the interaction between lactoferrin and kaempferol, as well as evaluate the in vitro anticancer properties of the lactoferrin-kaempferol complex. The results of the spectra experiments revealed that lactoferrin and kaempferol are capable of forming complexes to quench the endogenous fluorescence of lactoferrin. Further insight into the binding mechanism was gained through molecular docking and molecular dynamics simulations. These analyses suggest that both hydrophobic interactions and hydrogen bonding are essential factors in the interaction between lactoferrin and kaempferol. Furthermore, the MTT assay and apoptosis by flow cytometry were conducted, revealing a synergistic effect of kaempferol and lactoferrin on the inhibition of HeLa cell proliferation. The findings from this investigation could improve our understanding of lactoferrin's interaction with polyphenols and the role of the lactoferrin-kaempferol complex in inhibiting cancer cell proliferation.

摘要

乳铁蛋白和多酚是常见的天然功能化合物。它们之间的相互作用以及由此导致的功能活性变化受到了广泛关注。这项工作旨在研究乳铁蛋白与山奈酚之间的相互作用，并评估乳铁蛋白 - 山奈酚复合物的体外抗癌特性。光谱实验结果表明，乳铁蛋白和山奈酚能够形成复合物以淬灭乳铁蛋白的内源荧光。通过分子对接和分子动力学模拟进一步深入了解了结合机制。这些分析表明，疏水相互作用和氢键都是乳铁蛋白与山奈酚相互作用的重要因素。此外，进行了MTT测定和流式细胞术检测细胞凋亡，结果显示山奈酚和乳铁蛋白对抑制HeLa细胞增殖具有协同作用。这项研究的结果可以增进我们对乳铁蛋白与多酚相互作用以及乳铁蛋白 - 山奈酚复合物在抑制癌细胞增殖中作用的理解。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b2b1/11606874/1ed0fda4ff4e/FSN3-12-9046-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b2b1/11606874/61d54a5c88aa/FSN3-12-9046-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b2b1/11606874/cecfd555edc2/FSN3-12-9046-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b2b1/11606874/da86ada88bce/FSN3-12-9046-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b2b1/11606874/7285ab9fdc49/FSN3-12-9046-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b2b1/11606874/9abbd16d2da2/FSN3-12-9046-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b2b1/11606874/38c3af9a118e/FSN3-12-9046-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b2b1/11606874/2aed7deddb86/FSN3-12-9046-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b2b1/11606874/1ed0fda4ff4e/FSN3-12-9046-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b2b1/11606874/61d54a5c88aa/FSN3-12-9046-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b2b1/11606874/cecfd555edc2/FSN3-12-9046-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b2b1/11606874/da86ada88bce/FSN3-12-9046-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b2b1/11606874/7285ab9fdc49/FSN3-12-9046-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b2b1/11606874/9abbd16d2da2/FSN3-12-9046-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b2b1/11606874/38c3af9a118e/FSN3-12-9046-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b2b1/11606874/2aed7deddb86/FSN3-12-9046-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b2b1/11606874/1ed0fda4ff4e/FSN3-12-9046-g009.jpg

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