Triple helical collagen-like peptide interactions with selected polyphenolic compounds

Płońska‐Brzezińska, Marta E.; Bobrowska, Diana M.; Sharma, Amit; Rodziewicz, Paweł; Czyrko, Justyna; Brzeziński, Krzysztof

doi:10.1039/c5ra15469c

Cited by 14 publications

(12 citation statements)

References 81 publications

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“…And the Rpn value decreased to 0.098 when the dosage of proyanidin increased to 40%. It has been reported that the micro unfolding of the collagen triple helical structure rather than denaturing was observed under the effect of phenolic compound and the corresponding Rpn values decreased (27,(33)(34). Therefore, the decreasing of Rpn values here was probably attributed to the conformational change of collagen molecule, which agreed well with the investigation of AFM (globular aggregates shown in Figure 1e and f).…”

Section: Circular Dichroism (Cd) Studiessupporting

confidence: 88%

A Reconsideration of the Effect of Procyanidin on the Assembly of Collagen Type I

Wang

Jin

2018

Preprint

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In order to elucidating the exact effect mechanism of polyphenols on the assembly of collagen, the assembled architectures of collagen treated with different amounts of procyanidin (PA) were investigated in details. The assembled morphologies of collagen were greatly influenced by the content of PA according to atomic force microcopy (AFM) images.When the content of PA was more than 20% (w/w), the fibrillar morphologies were substituted by globular aggregates, which were driven by the intense hydrogen bonding action originating from PA. While the formation of the non-fibrous aggregates was due to the coiling and entangling of flexible collagen molecules rather than their gelatinization based on the appearance of typical adsorption peaks at 222nm and 197nm on circular dichroism (CD) spectra. After being crosslinked by glutaraldehyde (GA), not only the diameters but also the lengths of fibrils increased. Unfortunately, the fibrillogenesis was still inhibited when the collagen suffered from 20% PA firstly and then 4% GA. Conversely, the fibrous morphologies of the fibrils stabilized by 4% GA and then underwent 20% PA maintained well, in spite of accompanying with grievous intertwining. This difference was derived from the change of flexibilities of collagen before and after being crosslinked by GA. Additionally, the differential scanning calorimeter (DSC) analysis confirmed the PA had no positive effect on the improvement of thermal stability of hydrous collagen, whereas the denaturation temperature of hydrated collagen stabilized by 4% GA increased from 40 °C to 80 °C.

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Section: Circular Dichroism (Cd) Studiessupporting

confidence: 88%

A Reconsideration of the Effect of Procyanidin on the Assembly of Collagen Type I

Wang

Jin

2018

Preprint

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“…Three models were created for study; a wild-type, which is an extension to the unit-cell of the 4Z1R crystal structure of a collagen-like peptide [ 38 ], a model with a lysine and arginine side chain substituted between two polypeptide chains at residue positions 17 and 49 respectively, and a glucosepane cross-link between two polypeptide chains of the same collagen molecule at positions 17 and 49. Only one collagen molecule from the eight available was modified (with the exception to the wild-type) in the final extended unit cell.…”

Section: Methodsmentioning

confidence: 99%

Glucosepane is associated with changes to structural and physical properties of collagen fibrils

Nash

Notou

Lopez-Clavijo

et al. 2019

Matrix Biology Plus

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Collagen glycation, and in particular the formation of advanced glycation end-product (AGE) crosslinks, plays a central role in the ageing process and in many of the long-term complications of diabetes. Glucosepane, the most abundant and relevant AGE crosslink, has been suggested to increase the stiffness of tissue and reduce its solubility, although no evidence is available concerning the mechanisms. We have used a combination of computational and experimental techniques to study a collagen-rich tissue with a relatively simple organisation to further our understanding of the impact of glucosepane on the structural and physical properties of collagen fibrils. Our work shows that glucosepane levels increase dramatically in aged tendon tissue and are associated with the reduced density of collagen packing and increased porosity to water molecules. Our studies provide the basis to understand many of the tissue dysfunctions associated with ageing and diabetes across a range of different tissues types.

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“…The interactions between constituents in functional foods can potentially influence their biological activity. Many studies have revealed the interactions between phenolic compounds and other bioactive compounds, including proteins and peptides. − More importantly, the interaction between peptides and phenols can even improve the in vitro antioxidant capacity of DWMH . Apart from direct improvements in efficacy, the interactions between bioactive ingredients also enhance performance by optimizing their pharmacokinetic properties.…”

Section: Introductionmentioning

confidence: 99%

Coadministration with Tea Polyphenols Enhances the Neuroprotective Effect of Defatted Walnut Meal Hydrolysate against Scopolamine-Induced Learning and Memory Deficits in Mice

Sheng

Yang

Liu

et al. 2019

J. Agric. Food Chem.

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The present study aimed to investigate the combined effects of defatted walnut meal hydrolysate (DWMH) and tea polyphenols (TP) on learning improvement and to explain mechanistically why the combined treatments were more effective than either subject alone. In the step-down avoidance test and the Morris water maze test, codelivery of DWMH and TP was more effective than either individual supplement in reversing memory impairment in scopolamine-treated mice. Mixing with TP significantly facilitated the protective effects of DWMH or DWMH-derived peptides (cationic peptide P1 and anionic peptide P2) on H2O2-injured SH-SY5Y cells. Although combination treatment with TP and DWMH did not significantly alter systemic exposure to P1 or P2 in rats, it significantly increased the accumulation of the two peptides in the mouse brain. In addition, TP significantly improved cellular uptake of P1 and P2 by brain capillary endothelial cells, indicating that TP enhanced the blood–brain barrier permeation of DWMH-derived peptides. The proposed explanation for the advantage of combined treatment with TP and DWMH in reversing memory impairment was that TP enhanced both the protective effects of DWMH on nerve cells and the accumulation of DWMH in the brain. Our study can aid efforts to develop products and investigate the effects of nutrient combinations on brain disorders.

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Triple helical collagen-like peptide interactions with selected polyphenolic compounds

Abstract: Because collagen is the most abundant component of connective tissue, it is an excellent biomaterial in numerous medical applications.

Cited by 14 publications

References 81 publications

A Reconsideration of the Effect of Procyanidin on the Assembly of Collagen Type I

A Reconsideration of the Effect of Procyanidin on the Assembly of Collagen Type I

Glucosepane is associated with changes to structural and physical properties of collagen fibrils

Coadministration with Tea Polyphenols Enhances the Neuroprotective Effect of Defatted Walnut Meal Hydrolysate against Scopolamine-Induced Learning and Memory Deficits in Mice

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