Theoretical study of temperature induced transition and hyper stability of collagen mimics

Prasad, Onkar; Sinha, Leena; Gupta, Govind P.; Misra, Neeraj; Mehrotra, C.; Agnihotri, Ramesh C.; Lal, Jyotsana

doi:10.1016/j.polymer.2006.01.010

Cited by 7 publications

(4 citation statements)

References 19 publications

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“…Collagen as a protein was heat sensitive and would be denatured at a temperature called denaturation temperature (T d ) of approximately 40°C. Interestingly, it was found that the denaturation temperature of collagen decreased with increased concentrations (5,8,12,16 and 20 mg/ mL) suggesting that the molecular state of collagen was different in collagen solutions with different concentrations [10]. The reaction of the collagen molecules to temperature was therefore closely linked to the aggregation behavior of the collagen.…”

Section: Physicochemical Propertiesmentioning

confidence: 99%

“…Classifications may include fibril-forming, basement membrane, microfibrillar, anchoring fibrils, hexagonal network, discontinuous triple-helix [FACIT], transmembrane and fibril-associated collagen with multiplexes. A left-handed helical conformation is adopted by each collagen chain, and the three strands intertwine with a right-handed superhelical twist exhibiting a molecular weight as high as ~ 300 kDa [5]. As a natural polymer, collagen molecules appeared to entangle and accumulate in solution, resulting in a remarkable viscoelastic behaviour.…”

Section: Physicochemical Propertiesmentioning

confidence: 99%

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A review on collagen as a food supplement

Musayeva

Özcan

Kaynak

2022

jpt

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One of the most abundant proteins formed in the human body is collagen. It is responsible for the strength of body tissues in all cellular systems by establishing support networks. Collagen fibers are generally opaque and white, due to this reason they are easily recognized in the tissues. Collagen fibers, which are viscoelastic, have low extensibility and high tensile strength. The isoelectric point is around pH 5.8. Collagen is widely used as it helps blood coagulate, remodeling tissue. Although there are no known side effects, there is some concern about its role in inflammation, group-to-group variability, and possible disease transfection, given that animal-derived (natural) collagen is used in many clinical applications. Not every protein is of equal value, so not every collagen is of equal value. Thanks to its low molecular weight, hydrolyzed collagen is quickly digested by our body and enters our blood circulation. According to study, the most suitable type of collagen is the one in powder or liquid form for collagen peptides that can be easily absorbed and used by our body. It is necessary to rely on the most appropriate analysis technique to evaluate the quality feature. Techniques such as SEC, MS, HPLC and NMR are used to characterize complex peptide mixtures. Classical fibril-forming collagen includes collagen types I, II, III, V, and XI. These collagenes are characterized by their ability to aggregate into highly oriented supramolecular aggregates, forming fibrillar arrays with diameters between 25 and 400 nm. Being a natural protein and its technical characteristics, it is expected that development and consumption of collagen hydrolyzate will increase in the coming years. In this review, physical and chemical properties of collagen, types, pharmacology properties, quantity determination methods are briefly described.

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Section: Physicochemical Propertiesmentioning

confidence: 99%

Section: Physicochemical Propertiesmentioning

confidence: 99%

A review on collagen as a food supplement

Musayeva

Özcan

Kaynak

2022

jpt

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“…Collagen, the principal structural protein in connective tissue, is widely used in pharmaceutical production, food, cosmetic products, and the chemical industry because of its low antigenicity, good biocompatibility, and controlled biodegradability . These excellent biofunctionalities of collagen are mainly ascribed to its unique right‐handed helical conformation, which is supercoiled by three left‐handed α‐chains, exhibiting a molecular weight as high as 300 kDa . Both the long peptide chains and the high molecular weight endow collagen with an aggregated character.…”

Section: Introductionmentioning

confidence: 99%

Investigation on the interaction of collagen molecules in solution with different acetic acid concentrations

Yang

Deng

et al. 2017

J of Applied Polymer Sci

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Collagen solutions in the presence of 0.1-2.0M acetic acid (AA) were investigated to understand the interaction between collagen molecules and an acidic solvent. Fluorescence measurements of pyrene showed that the critical aggregation concentration (CAC) of collagen increased from 0.518 to 1.581 mg/mL for AA concentrations ranging from 0.1 to 2.0M, indicating that the aggregated state of collagen molecules was associated with AA concentration. The size of the collagen aggregates, determined by dynamic light scattering, demonstrated that their disaggregation was enhanced with increasing electrostatic repulsion between the collagen chains. The variations in the intrinsic viscosity and Huggins coefficient depended on the molecular interaction among the collagen molecules. Furthermore, the increased AA concentration has a different influence on the rigidity of collagen molecules above and below the CAC. This observation was manifested by the changes in the morphology of collagen molecules observed by atomic force microscopy.

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“…Natural and mature collagen is a rope-like molecule, which is composed of three-strand helicalwinding polypeptides (Shoulders & Raines, 2009). Each collagen chain adopts a left-handed helical conformation, and the three strands intertwine with a right-handed superhelical twist exhibiting an molecular weight of as high as ∼300 kDa (Prasad et al, 2006). Collagen, as an important biomaterial, has many applications in biomedical and pharmaceutical fields due to its weak antigenicity, biodegradability, biocompatibility and bioactivity (Jose, Thomas, Dean, & Nyairo, 2009;Kolodziejska, Sikorski, & Niecikowska, 1999;Lv, Feng, Hu, & Cui, 2005).…”

Section: Introductionmentioning

confidence: 99%