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The Inhibition Mechanisms of Three Structurally Different Salvianolic Acids on the Non-Enzymatic Glycation of Bovine Serum Albumin

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Abstract

The antiglycation mechanisms of three structurally different salvianolic acids (Sals) including salvianolic acid A (Sal-A), salvianolic acid B (Sal-B) and salvianolic acid C (Sal-C) were investigated using the bovine serum albumin (BSA)-fructose model. The results showed that the three compounds could inhibit the formation of glycation products, maintain protein structural stability, mitigate the development of amyloid fibrils and scavenge radicals. Notably, Sal-A possessed the highest anti-glycated activity compared with Sal-B and Sal-C. This may be related to the fact that Sal-A contained the most molecules of caffeic acid (Sal-A, Sal-B, and Sal-C possessing two, one, and zero caffeic acid units, respectively), and caffeic acid played a leading role in the antiglycation properties relative to Danshensu. Moreover, these compounds quenched the intrinsic fluorescence intensity of BSA in a static mode, with the binding constants in the order of Sal-A > Sal-B > Sal-C. Obviously, Sal-A possessed the strongest binding affinity among these compounds, which may be one of the reasons why it exhibited the optimal antiglycation capability. Furthermore, molecular docking demonstrated that the three Sals exerted protective effects on BSA by preventing glycation modification of lysine and arginine residues. These findings would provide valuable insights into the potential application of Sals for alleviating non-enzymatic glycation of protein.

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Data are available upon reasonable request.

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Funding

This work was supported by the National Natural Science Foundation of China (21506152), the Open Fund of Key Laboratory of Biotechnology and Bioresources Utilization (Dalian Minzu University), Ministry of Education (KF2023006), China, the Foundation of State Key Laboratory for Chemistry and Molecular Engineering of Medicinal Resources, Guangxi Normal University (CMEMR2022-B02).

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Author notes

  1. Guo Feng and Yu Yan contributed equally to this work. Dr. Mengfan Wang and Dr. Zhao Gao and Dr. Yinan Zhao are also the corresponding authors.

Authors and Affiliations

  1. School of Life Sciences, Tianjin University, Tianjin, 300072, PR China

    Guo Feng, Yu Yan, Mengfan Wang & Xin Peng

  2. Key Laboratory of Biotechnology and Bioresources Utilization of Ministry of Education, Dalian Minzu University, Dalian, 116600, Liaoning, PR China

    Zhao Gao, Yinan Zhao & Xin Peng

  3. State Key Laboratory for Chemistry and Molecular Engineering of Medicinal Resources, Guangxi Normal University, Guilin, 541004, Guangxi, PR China

    Xin Peng

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  1. Guo Feng
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  4. Zhao Gao
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Contributions

Guo Feng: Investigation, Software, Validation, Writing-original draft. Yu Yan: Investigation, Formal analysis, Validation. Mengfan Wang: Investigation, Formal analysis. Zhao Gao and Yinan Zhao: Funding acquisition, Resources. Xin Peng: Conceptualization, Methodology, Supervision, Funding acquisition, Writing-review & editing.

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Correspondence to Mengfan Wang, Zhao Gao, Yinan Zhao or Xin Peng.

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Feng, G., Yan, Y., Wang, M. et al. The Inhibition Mechanisms of Three Structurally Different Salvianolic Acids on the Non-Enzymatic Glycation of Bovine Serum Albumin. Plant Foods Hum Nutr (2024). https://doi.org/10.1007/s11130-024-01167-w

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