Application of Congo red dye as a molecular probe to investigate the kinetics and thermodynamics of the formation processes of arachin and conarachin nanocomplexes. (1st August 2022)
- Record Type:
- Journal Article
- Title:
- Application of Congo red dye as a molecular probe to investigate the kinetics and thermodynamics of the formation processes of arachin and conarachin nanocomplexes. (1st August 2022)
- Main Title:
- Application of Congo red dye as a molecular probe to investigate the kinetics and thermodynamics of the formation processes of arachin and conarachin nanocomplexes
- Authors:
- Rezende, Jaqueline de Paula
De Paula, Hauster Maximiler Campos
Freitas, Talma Duarte
Coelho, Yara Luiza
Da Silva, Luis Henrique Mendes
Pires, Ana Clarissa dos Santos - Abstract:
- Highlights: Peanut proteins (ARA or CON) interact with Congo red (CR) to form stable complexes. CON has a higher binding affinity toward CR than does ARA. Hydrophilic interactions were the main driving forces for [ A R A - C R ] 0 formation process. The formation of [ C O N - C R ] 0 was enthalpically and entropically driven. Transition complexes had a more structured conformation than their stable form. Abstract: The thermodynamics and kinetics of arachin-Congo red ( ARA - C R ) and conarachin-Congo red ( CON - C R ) interactions were studied using surface plasmon resonance. KCl led to a reduction of up to 55% in the values of the associated kinetic constants, but it had less influence on the dissociation rates (less than 12%). The change in ionic strength had little effect on the thermodynamic stability of the complexes, but it did reduce their affinities ( K b ( 25 ° C ) [ A R A - C R ] 0 from 3.52 to 2.44 × 10 3 M −1 and K b ( 25 ° C ) [ C O N - C R ] 0 from 15.1 to 12.5 × 10 3 M −1 ). The shielding of the electrical double layer favored ARA - C R hydrophilic interactions ( Δ H [ A R A - C R ] 0 0 decreased from −30.60 to −42.98 kJ mol −1 ). On the other hand, hydrophobic interactions came to dominate during the formation of [ C O N - C R ] 0 ( Δ H [ C O N - C R ] 0 0 increased from −11.21 to 28.34 kJ mol −1 and T Δ S 25 ° C [ C O N - C R ] 0 0 increased from 12.64 to 51.73 kJ.mol −1 ). The data presented here improve our understanding of plant-based proteinHighlights: Peanut proteins (ARA or CON) interact with Congo red (CR) to form stable complexes. CON has a higher binding affinity toward CR than does ARA. Hydrophilic interactions were the main driving forces for [ A R A - C R ] 0 formation process. The formation of [ C O N - C R ] 0 was enthalpically and entropically driven. Transition complexes had a more structured conformation than their stable form. Abstract: The thermodynamics and kinetics of arachin-Congo red ( ARA - C R ) and conarachin-Congo red ( CON - C R ) interactions were studied using surface plasmon resonance. KCl led to a reduction of up to 55% in the values of the associated kinetic constants, but it had less influence on the dissociation rates (less than 12%). The change in ionic strength had little effect on the thermodynamic stability of the complexes, but it did reduce their affinities ( K b ( 25 ° C ) [ A R A - C R ] 0 from 3.52 to 2.44 × 10 3 M −1 and K b ( 25 ° C ) [ C O N - C R ] 0 from 15.1 to 12.5 × 10 3 M −1 ). The shielding of the electrical double layer favored ARA - C R hydrophilic interactions ( Δ H [ A R A - C R ] 0 0 decreased from −30.60 to −42.98 kJ mol −1 ). On the other hand, hydrophobic interactions came to dominate during the formation of [ C O N - C R ] 0 ( Δ H [ C O N - C R ] 0 0 increased from −11.21 to 28.34 kJ mol −1 and T Δ S 25 ° C [ C O N - C R ] 0 0 increased from 12.64 to 51.73 kJ.mol −1 ). The data presented here improve our understanding of plant-based protein nanocarriers of small bioactive molecules. … (more)
- Is Part Of:
- Food chemistry. Volume 384(2022)
- Journal:
- Food chemistry
- Issue:
- Volume 384(2022)
- Issue Display:
- Volume 384, Issue 2022 (2022)
- Year:
- 2022
- Volume:
- 384
- Issue:
- 2022
- Issue Sort Value:
- 2022-0384-2022-0000
- Page Start:
- Page End:
- Publication Date:
- 2022-08-01
- Subjects:
- Plant-based protein -- Nanocarriers -- Transition complex -- Surface plasmon resonance -- Hydrophobic/hydrophilic balance
Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
664 - Journal URLs:
- http://www.sciencedirect.com/science/journal/03088146 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodchem.2022.132485 ↗
- Languages:
- English
- ISSNs:
- 0308-8146
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.284000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 21348.xml