Deciphering the non-covalent binding patterns of three whey proteins with rosmarinic acid by multi-spectroscopic, molecular docking and molecular dynamics simulation approaches

Lu, Yingcong; Zhao, Ru; Wang, Cuina

doi:10.1016/j.foodhyd.2022.107895

Cited by 59 publications

(24 citation statements)

References 66 publications

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“…The changes in the intensity of the absorption supported the complex’s formation between TF1 and three whey protein [ 49 ]. The results were consistent with previous findings, and it has been widely reported that polyphenols induced bathochromic-shift for whey proteins [ 50 , 51 ].…”

Section: Resultssupporting

confidence: 93%

Study on the Interaction Mechanism of Theaflavin with Whey Protein: Multi-Spectroscopy Analysis and Molecular Docking

Huang

Gao

et al. 2023

Foods

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The interaction mechanism of whey proteins with theaflavin (TF1) in black tea was analyzed using multi-spectroscopy analysis and molecular docking simulations. The influence of TF1 on the structure of bovine serum albumin (BSA), β-lactoglobulin (β-Lg), and α-lactoalbumin (α-La) was examined in this work using the interaction of TF1 with these proteins. Fluorescence and ultraviolet-visible (UV-vis) absorption spectroscopy revealed that TF1 could interact with BSA, β-Lg and α-La through a static quenching mechanism. Furthermore, circular dichroism (CD) experiments revealed that TF1 altered the secondary structure of BSA, β-Lg and α-La. Molecular docking demonstrated that the interaction of TF1 with BSA/β-Lg/α-La was dominated by hydrogen bonding and hydrophobic interaction. The binding energies were −10.1 kcal mol−1, −8.4 kcal mol−1 and −10.4 kcal mol−1, respectively. The results provide a theoretical basis for investigating the mechanism of interaction between tea pigments and protein. Moreover, the findings offered technical support for the future development of functional foods that combine tea active ingredients with milk protein. Future research will focus on the effects of food processing methods and different food systems on the interaction between TF1 and whey protein, as well as the physicochemical stability, functional characteristics, and bioavailability of the complexes in vitro or in vivo.

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Section: Resultssupporting

confidence: 93%

Study on the Interaction Mechanism of Theaflavin with Whey Protein: Multi-Spectroscopy Analysis and Molecular Docking

Huang

Gao

et al. 2023

Foods

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“…These results indicated that the polarity around Tyr and Trp residues was changed, the hydrophobicity of both the residues increased upon binding with LA, and the whey protein conformations were also changed . Similarly, Lu et al have reported that the addition of rosmarinic acid induced the blue shift of three whey proteins along with fluorescence intensity quenching, implying the alternations of the polarity of Trp and Tyr residues and their hydrophobicity . Moreover, the fluorescence intensity of Trp and Tyr decreased by a similar extent, implying that Trp and Tyr contributed equally to whey protein–LA interaction (Figure E,F).…”

Section: Resultsmentioning

confidence: 54%

Binding of Licochalcone A to Whey Protein Enhancing Its Antioxidant Activity and Maintaining Its Antibacterial Activity

Shen

Xue

Tan

et al. 2022

J. Agric. Food Chem.

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Incorporating LA into whey protein by forming whey protein isolate−LA (WPI−LA) and polymerized whey protein−LA (PWP−LA) complexes is a good way to maintain its bioactivity and improve its functional performance within food matrices. Herein, we found that WPI and PWP were able to interact with LA as suggested by multi-spectroscopy, molecular docking, and molecular dynamics simulations. The interaction between whey protein and LA was a spontaneous non-covalent binding process, while PWP had a higher affinity for LA than WPI, resulting from its more negatively binding free energy with LA. Hydrogen bonds, van der Waals forces, and electrostatic interactions were responsible for WPI−LA interactions. Hydrophobic forces, van der Waals, and hydrogen bonds positively accounted for PWP−LA interactions. The antioxidant activity of LA was improved by complexation with whey proteins as identified by DPPH and ABTS. The antimicrobial efficiency of LA was partially screened by complexation with whey protein with MIC values increased by seven-fold compared to free LA but successfully recovered to its original efficiency upon isolating it from the complex. This work demonstrates the promising antioxidant and antibacterial activities of the whey protein−LA complex and provides a good candidate for developing a new class of natural functional ingredients for food systems.

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“…Circular dichroism is a commonly used method for determining the secondary structure of proteins, 38 which takes advantage of the circular dichroism characteristic of optically active structures in proteins to investigate the effect of TA on the conformation of BSA molecules further. The results of the experiments were shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Insight into the interaction between tannin acid and bovine serum albumin from a spectroscopic and molecular docking perspective

Ning

Cao

et al. 2023

RSC Adv.

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Deciphering the non-covalent binding patterns of three whey proteins with rosmarinic acid by multi-spectroscopic, molecular docking and molecular dynamics simulation approaches

Cited by 59 publications

References 66 publications

Study on the Interaction Mechanism of Theaflavin with Whey Protein: Multi-Spectroscopy Analysis and Molecular Docking

Study on the Interaction Mechanism of Theaflavin with Whey Protein: Multi-Spectroscopy Analysis and Molecular Docking

Binding of Licochalcone A to Whey Protein Enhancing Its Antioxidant Activity and Maintaining Its Antibacterial Activity

Insight into the interaction between tannin acid and bovine serum albumin from a spectroscopic and molecular docking perspective

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