Next Article in Journal
Scrophularia Tenuipes Coss and Durieu: Phytochemical Composition and Biological Activities
Next Article in Special Issue
Membrane Phospholipids and Polyphosphates as Cofactors and Binding Molecules of SERPINA12 (vaspin)
Previous Article in Journal
Discovery, Synthesis, and Scale-up of Efficient Palladium Catalysts Useful for the Modification of Nucleosides and Heteroarenes
Previous Article in Special Issue
Evaluation of Isoflavones as Bone Resorption Inhibitors upon Interactions with Receptor Activator of Nuclear Factor-κB Ligand (RANKL)
Article

The Secondary Structure of a Major Wine Protein is Modified upon Interaction with Polyphenols

1
Department of Land, Environment, Agriculture and Forestry (TESAF), University of Padua, Viale dell’Università, 16, 35020 Legnaro (PD), Italy
2
Institute of Biomolecular Chemistry of CNR, Padua Unit, via Marzolo 1, 35131 Padua, Italy
3
Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, UK
4
Department of Chemical Sciences, University of Padua, Via Marzolo 1, 35131 Padua, Italy
5
Department of Agronomy, Food, Natural Resources Animals and Environment (DAFNAE), University of Padua, Viale dell’Università, 16, 35020 Legnaro (PD), Italy
*
Author to whom correspondence should be addressed.
These Authors contribute equally to this work.
Academic Editor: Derek J. McPhee
Molecules 2020, 25(7), 1646; https://doi.org/10.3390/molecules25071646
Received: 20 March 2020 / Revised: 1 April 2020 / Accepted: 1 April 2020 / Published: 3 April 2020
(This article belongs to the Special Issue Protein-Peptide and Protein-Small Molecule Interactions)
Polyphenols are an important constituent of wines and they are largely studied due to their antioxidant properties and for their effects on wine quality and stability, which is also related to their capacity to bind to proteins. The effects of some selected polyphenols, including procyanidins B1 and B2, tannic acid, quercetin, and rutin, as well as those of a total white wine procyanidin extract on the conformational properties of the major wine protein VVTL1 (Vitis vinifera Thaumatin-Like-1) were investigated by Synchrotron Radiation Circular Dichroism (SRCD). Results showed that VVTL1 interacts with polyphenols as demonstrated by the changes in the secondary (far-UV) and tertiary (near-UV) structures, which were differently affected by different polyphenols. Additionally, polyphenols modified the two melting temperatures (TM) that were found for VVTL1 (32.2 °C and 53.9 °C for the protein alone). The circular dichroism (CD) spectra in the near-UV region revealed an involvement of the aromatic side-chains of the protein in the interaction with phenolics. The data demonstrate the existence of an interaction between polyphenols and VVTL1, which results in modification of its thermal and UV denaturation pattern. This information can be useful in understanding the behavior of wine proteins in presence of polyphenols, thus giving new insights on the phenomena that are involved in wine stability. View Full-Text
Keywords: polyphenols; VVTL1; Synchrotron Radiation Circular Dichroism (SRCD); protein interaction; protein structure; wine polyphenols; VVTL1; Synchrotron Radiation Circular Dichroism (SRCD); protein interaction; protein structure; wine
Show Figures

Graphical abstract

  • Supplementary File 1:

    PDF-Document (PDF, 605 KiB)

  • Externally hosted supplementary file 1
    Doi: 10.5281/zenodo.3719387
    Link: https://zenodo.org/record/3719387#.XnTyR4hKiUk
    Description: Figure S1: Plot of secondary structure content of VVTL1 alone or in presence of 2 eq. of polyphenols (indicated) versus temperature. Secondary structure content was determined from SRCD data by CDApps [46] using CONTINLL algorithm [47]. VVTL1 concentration was 0.400 mg/mL. Figure S2: Melting curves of VVTL1 alone or in presence of 2 eq. of polyphenols (indicated). Curves were obtained plotting the ΔSRCD signal at 195 nm of VVTL1 versus temperature. Figure S3: Far-UV SRCD spectra (20 repeated scans collected at 20°C) of VVTL1 alone or in presence of different polyphenols. SRCD spectra were recorded using a Suprasil 0.02 cm cell (Hellma) filled with 60 µL of solution, integration time 1 s, 1 nm digital resolution, 39 nm/min scan speed and monochromator slit widths to 1.2 nm bandwidth. Protein concentration 0.400 mg/mL in MWS. Figure S4: Changes in the SRCD signal at 195 nm versus the number of scans of VVTL1 alone and in presence of polyphenols (indicated).
MDPI and ACS Style

Di Gaspero, M.; Ruzza, P.; Hussain, R.; Honisch, C.; Biondi, B.; Siligardi, G.; Marangon, M.; Curioni, A.; Vincenzi, S. The Secondary Structure of a Major Wine Protein is Modified upon Interaction with Polyphenols. Molecules 2020, 25, 1646. https://doi.org/10.3390/molecules25071646

AMA Style

Di Gaspero M, Ruzza P, Hussain R, Honisch C, Biondi B, Siligardi G, Marangon M, Curioni A, Vincenzi S. The Secondary Structure of a Major Wine Protein is Modified upon Interaction with Polyphenols. Molecules. 2020; 25(7):1646. https://doi.org/10.3390/molecules25071646

Chicago/Turabian Style

Di Gaspero, Mattia; Ruzza, Paolo; Hussain, Rohanah; Honisch, Claudia; Biondi, Barbara; Siligardi, Giuliano; Marangon, Matteo; Curioni, Andrea; Vincenzi, Simone. 2020. "The Secondary Structure of a Major Wine Protein is Modified upon Interaction with Polyphenols" Molecules 25, no. 7: 1646. https://doi.org/10.3390/molecules25071646

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop