Inhibition of amyloid formation of bovine hemoglobin by bioactive phenolic acids: an elaborate investigation into their binding properties with the protein using multi-spectroscopic and computational techniques

Studying the interactions of bioactive phenolic acids [ferulic acid (FA), caffeic acid (CA), and chlorogenic acid (CGA)] with the carrier protein bovine hemoglobin (BHb) helps to understand their modes of binding and transport, which affect their bioavailability. The protein-ligand complexes exhibit...

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Published inNew journal of chemistry Vol. 48; no. 27; pp. 12362 - 12386
Main Authors Lyndem, Sona, Giri, Piyusaranjan, , Bhatta, Anindita, Kumari, Kalpana, Jana, Madhurima, Singha Roy, Atanu
Format Journal Article
LanguageEnglish
Published Cambridge Royal Society of Chemistry 08.07.2024
Subjects
Acids
Assaying
Binding
Bioavailability
Biological activity
Cattle
Chlorogenic acid
Complexation
Dichroism
Enthalpy
Ferulic acid
Fluorescence
Hemoglobin
Hydrogen bonding
Infrared spectroscopy
Ligands
Phenolic acids
Proteins
Quenching
Turbidity
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Abstract Studying the interactions of bioactive phenolic acids [ferulic acid (FA), caffeic acid (CA), and chlorogenic acid (CGA)] with the carrier protein bovine hemoglobin (BHb) helps to understand their modes of binding and transport, which affect their bioavailability. The protein-ligand complexes exhibited binding constants ( K b ) in the range of 10 4 M −1 , indicating a reversible mode of association. BHb-CA complexation attenuated the inherent fluorescence of BHb (β 2 -Trp37 dominant fluorophore) through a static quenching mechanism. However, a combined (static and dynamic) quenching mechanism was observed for the BHb-FA/CGA complexes. In this study, the thermodynamic parameter, Δ G °, determined from fluorescence spectroscopy, was negative, suggesting that the complexation of BHb with phenolic acids was spontaneous. The negative change in enthalpy [Δ H ° = -(8.539 ± 1.331) kJ mol −1 , -(10.620 ± 1.028) kJ mol −1 , and -(8.637 ± 0.232) kJ mol −1 for BHb-FA, BHb-CA, BHb-CGA complexes, respectively] and positive entropy change [Δ S ° = + (63.862 ± 1.218) J mol −1 K −1 , +(67.108 ± 1.681) J mol −1 K −1 , and +(62.540 ± 1.058) J mol −1 K −1 for BHb-FA, BHb-CA, BHb-CGA complexes, respectively] indicated that hydrogen bonding and hydrophobic forces stabilized the complexes. Computational studies also illustrated similar interactive forces in BHb-ligand complexes. Changes around the microenvironment of the Trp residues in the binding process were verified using various spectral measurements. Circular dichroism and Fourier infrared spectroscopies illustrated a decrease in the α-helical content of BHb during complexation. Fibril inhibition properties of the ligands were verified using ThT assay, ANS binding studies, Congo Red assay, turbidity assay, Soret absorption measurements, and CD spectral measurements. The structure-activity relationship, binding affinity, and interactive forces between the protein and phenolic acids could explain the order of anti-fibrillation properties. Interactions of bioactive phenolic acids with BHb were investigated using spectroscopic methods along with their inhibitory potential against bovine hemoglobin amyloid formation in vitro .
AbstractList Studying the interactions of bioactive phenolic acids [ferulic acid (FA), caffeic acid (CA), and chlorogenic acid (CGA)] with the carrier protein bovine hemoglobin (BHb) helps to understand their modes of binding and transport, which affect their bioavailability. The protein–ligand complexes exhibited binding constants ( K b ) in the range of 10 4 M −1 , indicating a reversible mode of association. BHb–CA complexation attenuated the inherent fluorescence of BHb (β 2 -Trp37 dominant fluorophore) through a static quenching mechanism. However, a combined (static and dynamic) quenching mechanism was observed for the BHb–FA/CGA complexes. In this study, the thermodynamic parameter, Δ G °, determined from fluorescence spectroscopy, was negative, suggesting that the complexation of BHb with phenolic acids was spontaneous. The negative change in enthalpy [Δ H ° = –(8.539 ± 1.331) kJ mol −1 , –(10.620 ± 1.028) kJ mol −1 , and –(8.637 ± 0.232) kJ mol −1 for BHb–FA, BHb–CA, BHb–CGA complexes, respectively] and positive entropy change [Δ S ° = + (63.862 ± 1.218) J mol −1 K −1 , +(67.108 ± 1.681) J mol −1 K −1 , and +(62.540 ± 1.058) J mol −1 K −1 for BHb–FA, BHb–CA, BHb–CGA complexes, respectively] indicated that hydrogen bonding and hydrophobic forces stabilized the complexes. Computational studies also illustrated similar interactive forces in BHb–ligand complexes. Changes around the microenvironment of the Trp residues in the binding process were verified using various spectral measurements. Circular dichroism and Fourier infrared spectroscopies illustrated a decrease in the α-helical content of BHb during complexation. Fibril inhibition properties of the ligands were verified using ThT assay, ANS binding studies, Congo Red assay, turbidity assay, Soret absorption measurements, and CD spectral measurements. The structure–activity relationship, binding affinity, and interactive forces between the protein and phenolic acids could explain the order of anti-fibrillation properties.
Studying the interactions of bioactive phenolic acids [ferulic acid (FA), caffeic acid (CA), and chlorogenic acid (CGA)] with the carrier protein bovine hemoglobin (BHb) helps to understand their modes of binding and transport, which affect their bioavailability. The protein–ligand complexes exhibited binding constants (Kb) in the range of 104 M−1, indicating a reversible mode of association. BHb–CA complexation attenuated the inherent fluorescence of BHb (β2-Trp37 dominant fluorophore) through a static quenching mechanism. However, a combined (static and dynamic) quenching mechanism was observed for the BHb–FA/CGA complexes. In this study, the thermodynamic parameter, ΔG°, determined from fluorescence spectroscopy, was negative, suggesting that the complexation of BHb with phenolic acids was spontaneous. The negative change in enthalpy [ΔH° = –(8.539 ± 1.331) kJ mol−1, –(10.620 ± 1.028) kJ mol−1, and –(8.637 ± 0.232) kJ mol−1 for BHb–FA, BHb–CA, BHb–CGA complexes, respectively] and positive entropy change [ΔS° = + (63.862 ± 1.218) J mol−1 K−1, +(67.108 ± 1.681) J mol−1 K−1, and +(62.540 ± 1.058) J mol−1 K−1 for BHb–FA, BHb–CA, BHb–CGA complexes, respectively] indicated that hydrogen bonding and hydrophobic forces stabilized the complexes. Computational studies also illustrated similar interactive forces in BHb–ligand complexes. Changes around the microenvironment of the Trp residues in the binding process were verified using various spectral measurements. Circular dichroism and Fourier infrared spectroscopies illustrated a decrease in the α-helical content of BHb during complexation. Fibril inhibition properties of the ligands were verified using ThT assay, ANS binding studies, Congo Red assay, turbidity assay, Soret absorption measurements, and CD spectral measurements. The structure–activity relationship, binding affinity, and interactive forces between the protein and phenolic acids could explain the order of anti-fibrillation properties.
Studying the interactions of bioactive phenolic acids [ferulic acid (FA), caffeic acid (CA), and chlorogenic acid (CGA)] with the carrier protein bovine hemoglobin (BHb) helps to understand their modes of binding and transport, which affect their bioavailability. The protein-ligand complexes exhibited binding constants ( K b ) in the range of 10 4 M −1 , indicating a reversible mode of association. BHb-CA complexation attenuated the inherent fluorescence of BHb (β 2 -Trp37 dominant fluorophore) through a static quenching mechanism. However, a combined (static and dynamic) quenching mechanism was observed for the BHb-FA/CGA complexes. In this study, the thermodynamic parameter, Δ G °, determined from fluorescence spectroscopy, was negative, suggesting that the complexation of BHb with phenolic acids was spontaneous. The negative change in enthalpy [Δ H ° = -(8.539 ± 1.331) kJ mol −1 , -(10.620 ± 1.028) kJ mol −1 , and -(8.637 ± 0.232) kJ mol −1 for BHb-FA, BHb-CA, BHb-CGA complexes, respectively] and positive entropy change [Δ S ° = + (63.862 ± 1.218) J mol −1 K −1 , +(67.108 ± 1.681) J mol −1 K −1 , and +(62.540 ± 1.058) J mol −1 K −1 for BHb-FA, BHb-CA, BHb-CGA complexes, respectively] indicated that hydrogen bonding and hydrophobic forces stabilized the complexes. Computational studies also illustrated similar interactive forces in BHb-ligand complexes. Changes around the microenvironment of the Trp residues in the binding process were verified using various spectral measurements. Circular dichroism and Fourier infrared spectroscopies illustrated a decrease in the α-helical content of BHb during complexation. Fibril inhibition properties of the ligands were verified using ThT assay, ANS binding studies, Congo Red assay, turbidity assay, Soret absorption measurements, and CD spectral measurements. The structure-activity relationship, binding affinity, and interactive forces between the protein and phenolic acids could explain the order of anti-fibrillation properties. Interactions of bioactive phenolic acids with BHb were investigated using spectroscopic methods along with their inhibitory potential against bovine hemoglobin amyloid formation in vitro .
Author Bhatta, Anindita
Giri, Piyusaranjan
Lyndem, Sona
Jana, Madhurima
Singha Roy, Atanu
Kumari, Kalpana
AuthorAffiliation Department of Chemistry
Department of Bioscience and Bioengineering
North Eastern Hill University
National Institute of Technology
Indian Institute of Technology Guwahati
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Snippet Studying the interactions of bioactive phenolic acids [ferulic acid (FA), caffeic acid (CA), and chlorogenic acid (CGA)] with the carrier protein bovine...
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SubjectTerms Acids
Assaying
Binding
Bioavailability
Biological activity
Cattle
Chlorogenic acid
Complexation
Dichroism
Enthalpy
Ferulic acid
Fluorescence
Hemoglobin
Hydrogen bonding
Infrared spectroscopy
Ligands
Phenolic acids
Proteins
Quenching
Turbidity
Title Inhibition of amyloid formation of bovine hemoglobin by bioactive phenolic acids: an elaborate investigation into their binding properties with the protein using multi-spectroscopic and computational techniques
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