Interaction of flavan-3-ol derivatives and different caseins is determined by more than proline content and number of proline repeats

Bohin, Maxime C.; Vincken, Jean‐Paul; Westphal, Adrie H.; Tripp, Annelise M.; Dekker, P.; Hijden, H.T.W.M. van der; Gruppen, Harry

doi:10.1016/j.foodchem.2014.02.145

Cited by 25 publications

(27 citation statements)

References 26 publications

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“…The innerfilter effects refer to the absorbance of ligand with different dilution at the excitation or emission wavelength. The following equation adapted from Bohin et al [20] was used for estimating correct fluorescence:…”

Section: Fluorescence Spectrum Measurementsmentioning

confidence: 99%

“…When the inner-filter effect was excluded, any observed changes in fluorescence were likely related to either binding of protein with ligand, or collision effects [21]. The fluorescence spectra of l-tryptophan with various amounts of ligand were recorded according to the methods of Bohin et al [20] and van de Weert et al [21] for evaluating collision effects. Only on condition that the inner-filter and collision effects were demonstrated to be negligible can binding-induced phenomena be put forward.…”

Section: Fluorescence Spectrum Measurementsmentioning

confidence: 99%

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Binding interaction between rice glutelin and amylose: Hydrophobic interaction and conformational changes

Liu

Zhong

et al. 2015

International Journal of Biological Macromolecules

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Section: Fluorescence Spectrum Measurementsmentioning

confidence: 99%

Section: Fluorescence Spectrum Measurementsmentioning

confidence: 99%

Binding interaction between rice glutelin and amylose: Hydrophobic interaction and conformational changes

Liu

Zhong

et al. 2015

International Journal of Biological Macromolecules

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“…In addition to natural occurring agents, synthetic chemicals can also induce non-enzymatic collagen cross-linking (Bohin et al, 2014). The in vitro benefits of these chemical agents for the dentin-adhesive interface has been reported (Dos Santos et al, 2011a;b; Bedran-Russo et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

Potential role of surface wettability on the long-term stability of dentin bonds after surface biomodification

Leme

Vidal

Hassan

et al. 2015

Journal of Biomechanics

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Degradation of the adhesive interface contributes to the failure of resin composite restorations. The hydrophilicity of the dentin matrix during and after bonding procedures may result in an adhesive interface that is more prone to degradation over time. This study assessed the effect of chemical modification of dentin matrix on the wettability and the long-term reduced modulus of elasticity (Er) of the adhesive interfaces. Human molars were divided into groups according to the priming solutions: distilled water (control), 6.5% Proanthocyanidin-rich grape seed extract (PACs), 5.75% 1-ethyl-3-[3-dimethylaminopropyl] carbodiimide hydrochloride/1.4% n-hydroxysuccinimide (EDC/NHS) and 5% Glutaraldehyde (GA). The water-surface contact angle was verified before and after chemical modification of the dentin matrix. The demineralized dentin surface was treated with the priming solutions and restored with One Step Plus (OS) and Single Bond Plus (SB) and resin composite. The Er of the adhesive, hybrid layer and underlying dentin was evaluated after 24 h and 30 months in artificial saliva. The dentin hydrophilicity significantly decreased after application of the priming solutions. Aging significantly decreased the Er in the hybrid layer and underlying dentin of control groups. The Er of GA groups remained stable over time at the hybrid layer and underlying dentin. Significant higher Er was observed for PACs and EDC/NHS groups at the hybrid layer after 24 h. The decreased hydrophilicity of the modified dentin matrix likely influence the immediate mechanical properties of the hybrid layer. Dentin biomodification prevented substantial aging at the hybrid layer and underlying dentin after 30 months storage.

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“…FRET often becomes important when this radius is <10 nm. 30 R 0 for protein and PGG was estimated as described previously, 4 , 27 using a molar extinction coefficient of 10.6 mM –1 cm –1 . 31 R 0 was estimated to be 21.09 nm.…”

Section: Methodsmentioning

confidence: 99%

Resolubilization of Protein from Water-Insoluble Phlorotannin–Protein Complexes upon Acidification

Vissers

Blok

Westphal

et al. 2017

J. Agric. Food Chem.

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Marine phlorotannins (PhT) from Laminaria digitata might protect feed proteins from ruminal digestion by formation of insoluble non-covalent tannin–protein complexes at rumen pH (6–7). Formation and disintegration of PhT–protein complexes was studied with β-casein (random coil) and bovine serum albumin (BSA, globular) at various pH. PhT had similar binding affinity for β-casein and BSA as pentagalloyl glucose, as studied by fluorescence quenching. The affinity of PhT for both proteins was independent of pH (3.0, 6.0, and 8.0). In the presence of PhT, the pH range for precipitation of tannin–protein complexes widened to 0.5–1.5 pH units around the isoelectric point (pI) of the protein. Complete protein resolubilization from insoluble PhT–protein complexes was achieved at pH 7 and 2 for β-casein and BSA, respectively. It was demonstrated that PhT modulate the solubility of proteins at neutral pH and that resolubilization of PhT–protein complexes at pH deviating from pI is mainly governed by the charge state of the protein.

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Interaction of flavan-3-ol derivatives and different caseins is determined by more than proline content and number of proline repeats

Cited by 25 publications

References 26 publications

Binding interaction between rice glutelin and amylose: Hydrophobic interaction and conformational changes

Binding interaction between rice glutelin and amylose: Hydrophobic interaction and conformational changes

Potential role of surface wettability on the long-term stability of dentin bonds after surface biomodification

Resolubilization of Protein from Water-Insoluble Phlorotannin–Protein Complexes upon Acidification

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