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Interaction Mechanism between α-Lactalbumin and Caffeic Acid: A Multispectroscopic and Molecular Docking Study.

ABSTRACT: Caffeic acid (CA) is a phenolic acid found in a variety of foods. In this study, the interaction mechanism between α-lactalbumin (ALA) and CA was explored with the use of spectroscopic and computational techniques. The Stern-Volmer quenching constant data suggest a static mode of quenching between CA and ALA, depicting a gradual decrease in quenching constants with temperature rise. The binding constant, Gibbs free energy, enthalpy, and entropy values at 288, 298, and 310 K were calculated, and the obtained values suggest that the reaction is spontaneous and exothermic. Both in vitro and in silico studies show that hydrogen bonding is the dominant force in the CA-ALA interaction. Ser112 and Lys108 of ALA are predicted to form three hydrogen bonds with CA. The UV-visible spectroscopy measurements demonstrated that the absorbance peak A_280nm increased after addition of CA due to conformational change. The secondary structure of ALA was also slightly modified due to CA interaction. The circular dichroism (CD) studies showed that ALA gains more α-helical structure in response to increasing concentration of CA. The surface hydrophobicity of ALA is not changed in the presence of ethanol and CA. The present findings shown herein are helpful in understanding the binding mechanism of CA with whey proteins for the dairy processing industry and food nutrition security.

SUBMITTER: Al-Shabib NA

PROVIDER: S-EPMC10249380 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature

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Interaction Mechanism between α-Lactalbumin and Caffeic Acid: A Multispectroscopic and Molecular Docking Study.

Al-Shabib Nasser Abdulatif NA Khan Javed Masood JM Al-Amri Abdulaziz M AM Malik Ajamaluddin A Husain Fohad Mabood FM Sharma Prerna P Emerson Arnold A Kumar Vijay V Sen Priyankar P

ACS omega 20230522 22

Caffeic acid (CA) is a phenolic acid found in a variety of foods. In this study, the interaction mechanism between α-lactalbumin (ALA) and CA was explored with the use of spectroscopic and computational techniques. The Stern-Volmer quenching constant data suggest a static mode of quenching between CA and ALA, depicting a gradual decrease in quenching constants with temperature rise. The binding constant, Gibbs free energy, enthalpy, and entropy values at 288, 298, and 310 K were calculated, and ...[more]

PMID: 37305235

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Project description:DNA binding investigations are critical for designing better pharmaceutical compounds since the binding of a compound to dsDNA in the minor groove is critical in drug discovery. Although only one in vitro study on the DNA binding mode of apigenin (APG) has been conducted, there have been no electrochemical and theoretical studies reported. We hereby report the mechanism of binding interaction of APG and a new class of sulfonamide-modified flavonoids, apigenin disulfonamide (ADSAM) and apigenin trisulfonamide (ATSAM), with deoxyribonucleic acid (DNA). This study was conducted using multispectroscopic instrumentation techniques, which include UV-vis absorption, thermal denaturation, fluorescence, and Fourier transform infrared (FTIR) spectroscopy, and electrochemical and viscosity measurement methods. Also, molecular docking studies were conducted at room temperature under physiological conditions (pH 7.4). The molecular docking studies showed that, in all cases, the lowest energy docking poses bind to the minor groove of DNA and the apigenin-DNA complex was stabilized by several hydrogen bonds. Also, π-sulfur interactions played a role in the stabilization of the ADSAM-DNA and ATSAM-DNA complexes. The binding affinities of the lowest energy docking pose (schematic diagram of table of content (TOC)) of APG-DNA, ADSAM-DNA, and ATSAM-DNA complexes were found to be -8.2, -8.5, and -8.4 kcal mol-1, respectively. The electrochemical binding constants K b were determined to be (1.05 × 105) ± 0.04, (0.47 × 105) ± 0.02, and (8.13 × 105) ± 0.03 for APG, ADSAM, and ATSAM, respectively (all of the tests were run in triplicate and expressed as the mean and standard deviation (SD)). The K b constants calculated for APG, ADSAM, and ATSAM are in harmony for all techniques. As a result of the incorporation of dimethylsulfamate groups into the APG structure, in the ADSAM-dsDNA and ATSAM-dsDNA complexes, in addition to hydrogen bonds, π-sulfur interactions have also contributed to the stabilization of the ligand-DNA complexes. This work provides new insights that could lead to the development of prospective drugs and vaccines.

Dataset Information

Interaction Mechanism between α-Lactalbumin and Caffeic Acid: A Multispectroscopic and Molecular Docking Study.

Publications

Interaction Mechanism between α-Lactalbumin and Caffeic Acid: A Multispectroscopic and Molecular Docking Study.

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