β-lactoglobulin and resveratrol nanocomplex formation is driven by solvation water release.

Despite some thermodynamics studies about β-lactoglobulin (βLG) and resveratrol (RES) interactions, there is a gap regarding kinetics data about βLG-RES complex formation. Here, we determined the kinetic and thermodynamic parameters of βLG-RES interactions by using surface plasmon resonance (SPR). The kinetic association parameters were dependent on the 3D water structure present on the solvation shell of both interacting molecules.

Application of Congo red dye as a molecular probe to investigate the kinetics and thermodynamics of the formation processes of arachin and conarachin nanocomplexes.

The thermodynamics and kinetics of arachin-Congo red (ARA-CR) and conarachin-Congo red (CON-CR) 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 ( [Formula: see text] from 3.

Kinetic and thermodynamic of lactoferrin - Ethoxylated-nonionic surfactants supramolecular complex formation.

Understanding nonionic surfactant-protein interactions is fundamental from both technological and scientific points of view. However, there is a complete absence of kinetic data for such interactions. We employed surface plasmon resonance (SPR) to determine the kinetic and thermodynamic parameters of bovine lactoferrin-Brij58 interactions at various temperatures under physiological conditions (pH 7.

Thermodynamic and kinetic insights into the interactions between functionalized CdTe quantum dots and human serum albumin: A surface plasmon resonance approach.

To explore in vivo application of quantum dots (QDs), it is essential to understand the dynamics and energetics of interactions between QDs and proteins. Here, surface plasmon resonance (SPR) and molecular docking were employed to investigate the kinetics and thermodynamics of interactions between human serum albumin (HSA) and CdTe QDs (~3 nm) functionalized with mercaptopropionic acid (MPA) or thioglycolic acid (TGA). Kinetic analysis showed that HSA-QD interactions involved transition-complex formation.

Human serum albumin-resveratrol complex formation: Effect of the phenolic chemical structure on the kinetic and thermodynamic parameters of the interactions.

The thermodynamics and kinetics of binding between human serum albumin (HSA) and resveratrol (RES) or its analog (RESAn1) were investigated by surface plasmon resonance (SPR). The binding constant and the kinetic constants of association and dissociation indicated that RESAn1 has higher affinity toward HSA than does RES. The formation of these complexes was entropically driven ( [Formula: see text] , [Formula: see text]  KJ mol).

Surface plasmon resonance study of interaction between lactoferrin and naringin.

Lactoferrin (LF) is a glycoprotein that serves as a potential vehicle for small bioactive molecules in food. In an effort to improve this functionality, the kinetic and thermodynamic interaction of LF with naringin (NR) was studied by surface plasmon resonance (SPR). The results demonstrated that the association rate constant between LF and NR was 5.

Energetic parameters of β-casein/quercetin activated and thermodynamically stable complex formation accessed by Surface Plasmon Resonance.

Characterizing the energetics and molecular dynamics of binding between proteins and bioactive compounds is strategic. Using surface plasmon resonance, we demonstrated that β-casein (β-cas) and quercetin (Qct) form supramolecular complexes driven by an increase in entropy (ΔH° = 25.86 and TΔS° =53.

Lactoferrin-phenothiazine dye interactions: Thermodynamic and kinetic approach.

Life manifestation is mainly based on biopolymer-ligand molecular recognition; therefore, the elucidation of energy and speed associated with protein-ligand binding is strategic in understanding and modulating biological systems. In this study, the interactions between methylene blue (MB) or azure A (AZA) dyes and bovine lactoferrin (BLF) were investigated by surface plasmon resonance, fluorescence spectroscopy, and isothermal titration microcalorimetry. Despite the molecular similarities between the dyes, the BLF-AZA binding thermodynamic parameters (ΔG = -30.

Curcumin-micellar casein multisite interactions elucidated by surface plasmon resonance.

Determine the thermodynamic and kinetic parameters of interaction between micellar casein (MC) and curcumin (CUR) is useful for the application of MC-CUR systems in food products. We used surface plasmon resonance (SPR) and ultraviolet-visible spectrophotometry (UV-vis) to study the complex formation between MC obtained from skimmed milk and CUR, MC carrying capacity, and thermal protection for CUR at a pH of 6.6.

Kinetics and thermodynamics of bovine serum albumin interactions with Congo red dye.

To optimize the therapeutic applications of Congo red (CR), a potential inhibitor of protein aggregation, the kinetics and thermodynamics of the interactions between CR and a model protein need to be understood. We used surface plasmon resonance (SPR) and fluorescence techniques to determine the dynamics and thermodynamic parameters for the formation of complexes between CR and bovine serum albumin (BSA). CR interacts with BSA through a transition complex; the activation energy for association (E) was determined to be 35.