Towards the Importance of Fenugreek Proteins
Dilip Ghosh, Prasad Thakurdesai in Fenugreek, 2022
Various inter-molecular interactions in proteins result in their low molecular mobility, as well as high softening or melting temperature. In other words, once the protein is folded to its final native form, it is stabilized through hydrophobic and electrostatic interactions, hydrogen bonds, along with further strong covalent crosslinks. Softening of proteins requires their denaturation, meaning partial unfolding of structured native protein into an unstructured state with no or little fixed residual structures. Consequently, melting temperature of proteins could be considered as their denaturation temperature (Td). However, a complete unfolding into a fully amorphous structure may not occur as true melting means (Ricci et al., 2018). Considering that any changes in secondary, tertiary, or quaternary structures of proteins may refer to proteins denaturation, DSC not only gives insights into the differences between thermal characteristics of various proteins like legumes, but also could help to study the effects of various parameters on those attributes. Generally, denaturation of proteins is an endothermic process, owing to the heat they absorb to thermally unfold over a temperature range.
Raw veganism
Carlo Alvaro in Raw Veganism, 2020
Cooking denatures protein. Denaturation is a modification of the molecular structure of protein by heat or by an acid that destroys or diminishes its original properties and biological activity. Denaturation means that the molecular structure of proteins is modified and, as a result, the modified structure can be harmful for the body. Thus, “Most genetic diseases can be linked back to a protein that does not have the structure it should.”38 When food is cooked, resistant linkages are formed between the amino acid chains that the body cannot separate.39 Also, the Maillard reaction negatively affects the food (typically starches) generating prooxidants, carcinogens, and lowering the nutritional value of food.40 Furthermore, cooked fats can be rendered rancid and carcinogenic.41
Proteins in Cosmetics
E. Desmond Goddard, James V. Gruber in Principles of Polymer Science and Technology in Cosmetics and Personal Care, 1999
Rather surprisingly, although peptide charge and size have been separately studied for their influence on skin/hair substantivity and surfactant complexation, the charge/mass ratio has never been investigated as a specific parameter affecting the cosmetic properties of protein derivatives. Protein Denaturation
Green synthesis of ZnO-NPs using endophytic fungal extract of Xylaria arbuscula from Blumea axillaris and its biological applications
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2023
Lavanya Nehru, Gayathri Devi Kandasamy, Vanaraj Sekar, Mohammed Ali Alshehri, Chellasamy Panneerselvam, Abdulrahman Alasmari, Preethi Kathirvel
Protein denaturation is the primary cause of inflammation, and the potential of the nanoparticle’s protein denaturation was investigated as a part of an inquiry into the mechanism of anti-inflammatory action [55]. Protein denaturation is a detrimental process in which a functional protein loses its biological function as a result of structural modifications spurred on by external stimuli such as chemicals, heat, etc. [56]. Anti-inflammatory activity is one of the intriguing studies that attempt to examine the protective ability of NPs rather than their destructive aspect [55]. Therefore, it is necessary to investigate the anti-inflammatory potential of the biosynthesized nanoparticles at the onset of their application as a therapeutic agent. The maximum inhibition of protein denaturation obtained employing the ZnONPs was found to be 96.77 ± 0.23% at 500 µg/mL concentration which was extremely close to the obtained value from the standard drug diclofenac sodium 98.45 ± 0.66% at maximum concentration, as shown in Table 5. Similarly, biogenic ZnONPs synthesised using L. edodes were found to inhibit protein denaturation in a dose-dependent manner with a maximum inhibition % of about 86.45 ± 0.60 in a similar trend of inhibition exhibited by diclofenac [57].
Histological findings in resected leiomyomas following MR-HIFU treatment, single-institution data from seven patients with unfavorable focal therapy
Published in International Journal of Hyperthermia, 2023
Antti Viitala, Michael Gabriel, Kirsi Joronen, Gaber Komar, Antti Perheentupa, Teija Sainio, Jutta Huvila, Pekka Pikander, Pekka Taimen, Roberto Blanco Sequeiros
As the ECM is heated, denaturation of collagen is feasible at temperatures and time spans encountered during MR-HIFU [10]. Some changes in the collagen structure may be reversible, but at higher temperatures irreversible changes occur [10]. The denaturation rate is known to depend on temperature, mechanical load, hydration, chemical environment and amount of cross-linking (maturity) [10]. Ex vivo bovine tendons, which have high collagen content, shrink when heated [36]. The amount of shrinkage depends on the temperature and exposure time, while the proportion of denatured collagen fibrils increases with shrinkage [36]. Despite the initial shrinking, heat-treated tendons lose their mechanical strength and become easier to stretch [36]. Typical shrinkage temperature of mammalian collagens is known to be around 65–67 °C [37].
TiO2 nanoparticles: green synthesis, characterization, and investigation of antimicrobial properties, and developmental toxicity in zebrafish (Danio rerio) embryos
Published in Drug and Chemical Toxicology, 2023
Rajaduraipandian Subramanian, Mohemedibrahim Ponnanikajamideen, Rapael Samuel Rajendran, Mohammed Ali Alshehri, Abdulrahman Alasmari, Chellasamy Panneerselvam, Selvendiran Periyasamy
In the present study, both TiO2 and G-TiO2 NPs showed inhibition of protein (albumin) denaturation, indicating that both of them were effective in inhibiting the heat-induced albumin denaturation (Figure 7(B)). Denaturation of tissue proteins is a well-known cause of inflammation, and the formation of autoantigens as a result of in vivo protein denaturation is frequently found in inflammatory diseases like arthritis. Denaturation is thought to be caused by changes in electrostatic, hydrogen, hydrophobic, and disulfide bonding (Grant et al.1970). Therefore, the efficacy of TiO2 and G-TiO2 NPs to inhibit protein (albumin) denaturation ascertains the anti-inflammatory potential of both TiO2 and G-TiO2 NPs. Anti-inflammatory medications could benefit from agents that prevent protein denaturation.
Related Knowledge Centers
- Acid
- Biochemistry
- Inorganic Compound
- Nucleic Acid
- Organic Compound
- Protein
- Protein Quaternary Structure
- Protein Secondary Structure
- Protein Tertiary Structure
- Native State