Structural Properties of Colloidal Complexes between Condensed Tannins and Polysaccharide Hyaluronan

Carn, Florent; Guyot, Sylvain; Baron, Alain; Pérez, Javier; Buhler, Eric; Zanchi, D.

doi:10.1021/bm201674n

Cited by 44 publications

(26 citation statements)

References 22 publications

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“…The determination of DPn showed differences in hairy regions for binding to highly polymerized procyanidins DP30, unlike procyanidins DP9. The length of procyanidins DP30 facilitated aggregates formation (Carn et al, 2012). Procyanidins DP30 are a polymer more non-uniform than procyanidins DP9 (Le Bourvellec, Picot, & Renard, 2006).…”

Section: Discussionmentioning

confidence: 99%

Neutral sugar side chains of pectins limit interactions with procyanidins

Watrelot¹,

Bourvellec²,

Imberty³

et al. 2014

Carbohydrate Polymers

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Interactions between seven hairy regions of pectins, rhamnogalacturonans II and arabinogalactan-proteins and procyanidins with different average degrees of polymerization, low (DP9) and high (DP30), were investigated by isothermal titration calorimetry and absorption analysis to study the impact of neutral sugar side chains of pectins on these associations. Associations between pectic fractions and procyanidins involved hydrophobic interactions and hydrogen bonds. No difference in association constants between various hairy regions and procyanidins DP9 was found. Nevertheless, arabinan chains showed lower association constants, and hairy regions of pectins with only monomeric side chains showed higher association with procyanidin DP30. Only very low affinities were obtained with rhamnogalacturonans II and arabinogalactan-proteins. Aggregation could be observed only with the procyanidins of DP30 and the protein-rich arabinogalactan-protein. Associations were obtained at both degrees of polymerization of the procyanidins, but differed depending on neutral sugar composition and the structure of pectic fractions.

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Section: Discussionmentioning

confidence: 99%

Neutral sugar side chains of pectins limit interactions with procyanidins

Watrelot¹,

Bourvellec²,

Imberty³

et al. 2014

Carbohydrate Polymers

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“…On the contrary, interactions of proanthocyanidins with cell-walls appear to be a rapid, direct binding event. Polysaccharides do not collapse nor form closely packed aggregates in the presence of proanthocyanidins, but create either loose oligomers or microgels that are even less compact than single polysaccharide coils (Carn et al, 2012). The difference is easily observable already by moderate centrifugation, where proanthocyanidin-protein micelles are found in the pellet, while proanthocyanidin-polysaccharide complexes remain stable even at ultracentrifugation of 8 Â 10 5 g. The explanation of this difference is in the physical properties of proteins and polysaccharides.…”

Section: Non-covalent Interactionsmentioning

confidence: 99%

Interactions between polyphenols and polysaccharides: Mechanisms and consequences in food processing and digestion

Renard

Watrelot

Bourvellec

2017

Trends in Food Science & Technology

203

136

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Interactions between polyphenols and polysaccharides: Mechanisms and consequences in food processing and digestion. a b s t r a c t Background: Interactions between intracellular polyphenols and plant cell-walls have received little attention, due to analytical limitations. It was difficult until recently to analyse the most implicated polyphenols, which are proanthocyanidins (aka condensed tannins), and because these weak interactions were too low for quantification. They are becoming recognized as a factor to understand extractability, functional and health effects of polyphenols. Scope and approach: New approaches that have been used since the turn of the century are binding isotherms and isothermal titration calorimetry. They allow to investigate specifically these interactions, quantify the affinities between cell-walls and polyphenols as well as the impact of fruit maturation or processing, and the consequences on the finished beverages and food. This review will highlight results on this topic since 2001. Key findings and conclusions: The most common polyphenols are phenolic acids and oligo or polymeric flavanols (proanthocyanidins), located inside the vacuole in intact plant cells. The proanthocyanidins bind spontaneously to the plant cell-wall polysaccharides through plant tissue disruption, for example during grinding, mastication or thermal treatments, etc. The highest affinity is observed with pectins, which may help explain some of the effects of maturation on polyphenol extractability, e.g. in wine making. Presence of proanthocyanidins together with the cell-walls in the lower gut further impacts on the production of colonic metabolites. This has profound consequences on the extractability and bioavailability of the polyphenols, on the functional characteristics of extracted polysaccharides, and on the fermentation kinetics of dietary fibers and polyphenols.

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“…Each frame was first angularly averaged and the final spectrum and experimental error were obtained by averaging over all frames and subtracting the pure solvent spectrum from the sample spectrum. Intensities were scaled using the scattering of water 35 . Data analysis was based on fitting the scattering curve to an appropriate model by a least-squares method using software provided by NIST 36 (NIST SANS Analysis version 7.0 on IGOR).…”

Section: Methodsmentioning

confidence: 99%

Genetic manipulation of iron biomineralization enhances MR relaxivity in a ferritin-M6A chimeric complex

Radoul

Lewin

Cohen

et al. 2016

Sci Rep

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Ferritin has gained significant attention as a potential reporter gene for in vivo imaging by magnetic resonance imaging (MRI). However, due to the ferritin ferrihydrite core, the relaxivity and sensitivity for detection of native ferritin is relatively low. We report here on a novel chimeric magneto-ferritin reporter gene – ferritin-M6A – in which the magnetite binding peptide from the magnetotactic bacteria magnetosome-associated Mms6 protein was fused to the C-terminal of murine h-ferritin. Biophysical experiments showed that purified ferritin-M6A assembled into a stable protein cage with the M6A protruding into the cage core, enabling magnetite biomineralisation. Ferritin-M6A-expressing C6-glioma cells showed enhanced (per iron) r2 relaxivity. MRI in vivo studies of ferritin-M6A-expressing tumour xenografts showed enhanced R2 relaxation rate in the central hypoxic region of the tumours. Such enhanced relaxivity would increase the sensitivity of ferritin as a reporter gene for non-invasive in vivo MRI-monitoring of cell delivery and differentiation in cellular or gene-based therapies.

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Structural Properties of Colloidal Complexes between Condensed Tannins and Polysaccharide Hyaluronan

Cited by 44 publications

References 22 publications

Neutral sugar side chains of pectins limit interactions with procyanidins

Neutral sugar side chains of pectins limit interactions with procyanidins

Interactions between polyphenols and polysaccharides: Mechanisms and consequences in food processing and digestion

Genetic manipulation of iron biomineralization enhances MR relaxivity in a ferritin-M6A chimeric complex

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