Study of non‐covalent complexation between catechin derivatives and peptides by electrospray ionization mass spectrometry

Sarni‐Manchado, Pascale; Cheynier, Véronique

doi:10.1002/jms.321

Cited by 55 publications

(34 citation statements)

References 75 publications

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“…It is still unknown which specific amino acids are involved in collagen interaction with catechins, and if there is any covalent bond formation between the PACs and collagen. Stronger interaction between galloylated catechins and a peptide (composed mainly of proline) was observed when compared to non-galloylated compounds [17], supporting the greater interaction between EGCG, ECG, GCG and CG observed in the present study. Catechins might interact with the pyrrolidine ring present in proline, contributing to form hydrophobic bonds to collagen.…”

Section: Discussionsupporting

confidence: 85%

Galloyl moieties enhance the dentin biomodification potential of plant-derived catechins

et al. 2014

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Proanthocyanidin (PAC) rich plant-derived agents have been shown to enhance dentin biomechanical properties and resistance to collagenase degradation. This study systematically investigated the interaction of chemically well-defined monomeric catechins with dentin extracellular matrix components by evaluating dentin mechanical properties as well as activities of matrix metalloproteinases (MMPs) and cysteine-cathepsins (CTs). Demineralized dentin beams (n = 15) were incubated for 1 hr with 0.65% (+)-catechin (C), (−)-catechin gallate (CG), (−)-gallocatechin gallate (GCG), (−)-epicatechin (EC), (−)-epicatechin gallate (ECG), (−)-epigallocatechin (EGC), and (−)-epigallocatechin-3-gallate (EGCG). Modulus of elasticity (E) and E fold increase were determined, comparing specimens at baseline and after treatment. Biodegradation rates were assessed by differences in percentage of dry mass before and after incubation with bacterial collagenase. The inhibition of MMP-9 and CT-B by 0.65%, 0.065% and 0.0065% of each catechin was determined using fluorimetric proteolytic assay kits. All monomeric catechins led to a significant increase in E. EGCG showed the highest E fold increase, followed by ECG, CG and GCG. EGCG, ECG, GCG and CG significantly lowered biodegradation rates and inhibited both MMP-9 and CT-B at a concentration of 0.65%. Overall, the 3-O-galloylated monomeric catechins are clearly more potent than their non-galloylated analogues in improving dentin mechanical properties, stabilizing collagen against proteolytic degradation, and inhibiting the activity of MMPs and CTs. The results indicate that galloylation is a key pharmacophore in the monomeric and likely also in the oligomeric PACs that exhibit high cross-linking potential for dentin extracellular matrix.

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Section: Discussionsupporting

confidence: 85%

Galloyl moieties enhance the dentin biomodification potential of plant-derived catechins

et al. 2014

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“…In fact, for the interaction with 0.06 mg.mL -1 of ECG (at 0.4 mg.mL -1 of GTE), the ECG was completely bound to salivary proteins while at a similar concentration of EGCG it was not the case. The higher interaction of ECG in comparison to EGCG has been previously observed for the interaction with a proline-rich peptide by ESI-MS studies 51 . For the interactions with TR146 cell line and with the TR146MuSP model it was observed an increased binding of each compound along with their initial concentration.…”

Section: Interaction Of Phenolic Compounds (Structure-and Concentratisupporting

confidence: 65%

“…So, it seems that the molecules of these flavanols attain an equilibrium at a specific concentration between the unbound and bound molecules, and therefore there is not a complete interaction with all the molecules available, even for the lowest concentration. The previously referred self-association of these compounds could also justify this equilibrium 51 .…”

Section: Interaction Of Phenolic Compounds (Structure-and Concentratimentioning

confidence: 75%

Oral interactions between a green tea flavanol extract and red wine anthocyanin extract using a new cell-based model: insights on the effect of different oral epithelia

Soares

Brandão

et al. 2020

Sci Rep

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Victor de freitas Phenolic compounds (PC) are linked to astringency sensation. Astringency studies typically use simple models, with pure PC and/or proteins, far from what is likely to occur in the oral cavity. Different oral models have been developed here, comprising different oral epithelia (buccal mucosa (TR146) and tongue (HSC-3)) and other main oral constituents (human saliva and mucosal pellicle). These models, were used to study the interaction with two PC extracts, one rich in flavanols (a green tea extract) and one rich in anthocyanins (a red wine extract). It was observed that within a family of PC, the PC seem to have a similar binding to both TR146 and HSC-3 cell lines. When the oral constituents occur altogether, flavanols showed a higher interaction, driven by the salivary proteins. Conversely, anthocyanins showed a lower interaction when the oral constituents occur altogether, having a higher interaction only with oral cells. Epigallocatechin gallate, epicatechin gallate, epigallocatechin-3-O(3-O-methyl) gallate were the flavanols with the highest interaction. For the studied anthocyanins (delphinidin-3-glucoside, peonidin-3-glucoside, petunidin-3-glucoside and malvidin-3-glucoside), there was not a marked difference on their interaction ability. Overall, the results support that the different oral constituents can have a different function at different phases of food (PC) intake. These differences can be related to the perception of different astringency sub-qualities.

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“…IM-MS is an emerging analytical method that retains weak non-covalent interactions in the gas-phase and maintains protein conformations from solution phase (Konermann and Douglas, 1998 ; Sarni-Manchado and Cheynier, 2002 ; Wyttenbach and Bowers, 2011 ; Abzalimov et al, 2012 ). The IM-MS study presented here reinforces that soluble αSA53T undergoes a structural transition from natively unfolded to more compact amyloidogenic conformations at an early stage of aggregation, as measured by changes in CCSs.…”

Section: Discussionmentioning

confidence: 99%

Exploring the Structural Diversity in Inhibitors of α-Synuclein Amyloidogenic Folding, Aggregation, and Neurotoxicity

2018

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Aggregation of α-Synuclein (αS) protein to amyloid fibrils is a neuropathological hallmark of Parkinson's disease (PD). Growing evidence suggests that extracellular αS aggregation plays a pivotal role in neurodegeneration found in PD in addition to the intracellular αS aggregates in Lewy bodies (LB). Here, we identified and compared a diverse set of molecules capable of mitigating protein aggregation and exogenous toxicity of αSA53T, a more aggregation-prone αS mutant found in familial PD. For the first time, we investigated the αS anti-amyloid activity of semi-synthetic flavonoid 2′, 3′, 4′ trihydroxyflavone or 2-D08, which was compared with natural flavones myricetin and transilitin, as well as such structurally diverse polyphenols as honokiol and punicalagin. Additionally, two novel synthetic compounds with a dibenzyl imidazolidine scaffold, Compound 1 and Compound 2, were also investigated as they exhibited favorable binding with αSA53T. All seven compounds inhibited αSA53T aggregation as demonstrated by Thioflavin T fluorescence assays, with modified fibril morphology observed by transmission electron microscopy. Ion mobility-mass spectrometry (IM-MS) was used to monitor the structural conversion of native αSA53T into amyloidogenic conformations and all seven compounds preserved the native unfolded conformations of αSA53T following 48 h incubation. The presence of each test compound in a 1:2 molar ratio was also shown to inhibit the neurotoxicity of preincubated αSA53T using phaeochromocytoma (PC12) cell viability assays. Among the seven tested compounds 2-D08, honokiol, and the synthetic Compound 2 demonstrated the highest inhibition of aggregation, coupled with neuroprotection from preincubated αSA53T in vitro. Molecular docking predicted that all compounds bound near the lysine-rich region of the N-terminus of αSA53T, where the flavonoids and honokiol predominantly interacted with Lys 23. Overall, these findings highlight that (i) restricted vicinal trihydroxylation in the flavone B-ring is more effective in stabilizing the native αS conformations, thus blocking amyloidogenic aggregation, than dihydroxylation aggregation in both A and B-ring, and (ii) honokiol, punicalagin, and the synthetic imidazolidine Compound 2 also inhibit αS amyloidogenic aggregation by stabilizing its native conformations. This diverse set of molecules acting on a singular pathological target with predicted binding to αSA53T in the folding-prone N-terminal region may contribute toward novel drug-design for PD.

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Study of non‐covalent complexation between catechin derivatives and peptides by electrospray ionization mass spectrometry

Cited by 55 publications

References 75 publications

Galloyl moieties enhance the dentin biomodification potential of plant-derived catechins

Galloyl moieties enhance the dentin biomodification potential of plant-derived catechins

Oral interactions between a green tea flavanol extract and red wine anthocyanin extract using a new cell-based model: insights on the effect of different oral epithelia

Exploring the Structural Diversity in Inhibitors of α-Synuclein Amyloidogenic Folding, Aggregation, and Neurotoxicity

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