Stabilization of collagen using plant polyphenol: Role of catechin

Madhan, Balaraman; Subramanian, V.; Rao, Jonnalagadda Raghava; Nair, Balachandran Unni; Ramasami, T.

doi:10.1016/j.ijbiomac.2005.08.005

Cited by 176 publications

(143 citation statements)

References 39 publications

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“…Therefore, MFCF did not collapse when it was immersed in a solution with a higher temperature. Additionally, Ts of MFCF (79.3°C) was also higher than that of collagen film modified by catechin (70°C) (Madhan et al 2005), collagen film modified by curcumin (78°C) (Gopinath et al 2004). …”

Section: Thermal Propertiesmentioning

confidence: 88%

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Modification of fish skin collagen film and absorption property of tannic acid

et al. 2011

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Fish collagen is a biomacromolecule material and is usually used as a clarifying agent. However, fish collagen is not recyclable, and sedimentation usually occurs in the clarification process using fish collagen so that the filtration process is inevitable. This work aimed to provide a recyclable modified fish skin collagen film (MFCF) for adsorption of tannic acids. The collagen from channel catfish skin was extracted and used for preparation of the fish skin collagen film (FCF) and MFCF. The result indicated that the mechanical properties of MFCF were improved by addition of 2 ml/L glycerol, 6 ml/L polyvinyl alcohol (PVA) and 2 ml/L glutaraldehyde in 15 g/L collagen solution. As the most important property of adsorption material, the hydroscopicity of MFCF was only 54%, significantly lower than that of FCF (295%). Therefore, MFCF would not collapse in water. The infrared and thermal properties of MFCF were also investigated in this work. Results indicated that, in comparison to FCF, the physical and chemical properties of MFCF had been improved significantly. MFCF had higher shrink temperature (79.3°C) and it did not collapse in distilled water at normal temperature. Furthermore, absorption and desorption properties of tannic acid were studied. MFCF showed good capability of absorption and desorption of tannic acid, which leaded to the suggestion that MFCF could have potential applications in adsorption material.

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Section: Thermal Propertiesmentioning

confidence: 88%

“…It has been applied in the field of pharmaceutical, food processing and tanning industries (Madhan et al 2005) for its potential antiviral, antibacterial and antiparasitic effects and antioxygenic property. However, some extracts of plants contain excess tannins which usually debase the quality of those products.…”

Section: Introductionmentioning

confidence: 99%

Modification of fish skin collagen film and absorption property of tannic acid

et al. 2011

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“…Here, we establish the spectral shape of this component and demonstrate its utility for studying hierarchic assembly. As collagen solutions are most often analyzed under conditions in which fibrillogenesis is inhibited (19,(34)(35)(36)(37)(38)(39)(40)(41)(42), this signal has not previously been extensively described or studied. However, given the wide accessibility of CD spectroscopy, the identification of a collagen-fibril-associated spectrum presents opportunities to study collagen fibrillogenesis and associated structural transitions in solution.…”

Section: Introductionmentioning

confidence: 99%

Circular Dichroism Spectroscopy of Collagen Fibrillogenesis: A New Use for an Old Technique

Drzewiecki

Grisham

Parmar

et al. 2016

Biophysical Journal

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Type-I collagen assembles in a stepwise, hierarchic fashion from the folding of the triple helix to the assembly of fibrils into fibers. The mature assembled fibers are crucial for tissue structure and mechanics, cell interactions, and other functions in vivo. Although triple helix folding can be followed with the use of optical methods such as circular dichroism (CD) spectroscopy, fibrillogenesis is typically measured by alternative methods such as turbidity, rheology, and microscopy. Together, these approaches allow for investigation of the mechanical properties and architectures of collagen-based scaffolds and excised tissues. Herein, we demonstrate that CD spectroscopy, a technique that is used primarily to evaluate the secondary structure of proteins, can also be employed to monitor collagen fibrillogenesis. Type-I collagen suspensions demonstrated a strong, negative ellipticity band between 204 and 210 nm under conditions consistent with fibrillogenesis. Deconvolution of CD spectra before, during, and after fibrillogenesis identified a unique fibril spectrum distinct from triple helix and random coil conformations. The ability to monitor multiple states of collagen simultaneously in one experiment using one modality provides a powerful platform for studying this complex assembly process and the effects of other factors, such as collagenases, on fibrillogenesis and degradation.

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“…They have had extensive applications in the field of pharmaceutical, food processing and tanning industries. Their ability to form complexes with proteins or related biopolymers has been correlated with some protection of the plants from predators such as animals, insects and microbes (Madhan, Subramanian, Rao, Nair, & Ramasami, 2005). In this research, gallic acid and rutin were used as the cross-linking agents to modify the gelatin gels.…”

Section: Introductionmentioning

confidence: 99%