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Towards the Importance of Fenugreek Proteins
Published in Dilip Ghosh, Prasad Thakurdesai, 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.
Serum Keratan Sulfate Concentration as a Measure of the Catabolism of Cartilage Proteoglycans
Published in Thomas F. Kresina, Monoclonal Antibodies, Cytokines, and Arthritis, 2020
Eugene J.-M. A. Thonar, James M. Williams, Brian A. Maldonado, Mary Ellen Lenz, Thomas J. Schnitzer, Giles V. Campion, Klaus E. Kuettner, M. Barry, E. Sweet
The development of immunoassays to quantify the different constituents of cartilage PGs has led to a number of important advances by enabling researchers to address questions that would otherwise have remained unanswered. The advantages of using a highly sensitive and specific immunoassay for quantitative analysis are immediately obvious, but the dangers associated with equating measure of epitope recognized by an antibody with amount of protein or glycosaminoglycan present have often been ignored. Accurate quantification of CS- or KS-related epitopes is usually less difficult to achieve than that of some protein constituents. The HA binding region, for example, must first be denatured to prevent it from binding to HA, link protein, or other HA binding region molecules; such interactions have been shown to result in the masking of epitopes (27). Denaturation is easy to achieve, but the need to remove the denaturing agent, which can denature the antibody or suppress antigen-antibody interaction, is a complicating factor.
Transport of Radiolabeled Enzymes
Published in Lelio G. Colombetti, Biological Transport of Radiotracers, 2020
The most convenient procedure for protein/enzyme tritiation is the exchange of a hydrogen-3 ion supplied by tritiated water that is diluted in an organic solvent in the presence of a catalyst. The risk of protein denaturation seems very small. Evans et al.,11 Wilzbach,12 Means,13 and Bailey and Knowles14 described labeling procedures. Endert15 suggested the use of HPLC techniques for the separation of radiochemical impurities.
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].
Production of active human FGF21 using tobacco mosaic virus-based transient expression system
Published in Growth Factors, 2021
Jieying Fan, Yunpeng Wang, Shuang Huang, Shaochen Xing, Zhengyi Wei
Although FGF21 exists widely among vertebrates, its expression level is rather low, and cannot be extracted for mass production to meet the increasing demand in clinical application. Therefore, it remains the major challenge for the efficient large-scale production of FGF21. The inclusion bodies have been the main problem in E. coli system that the bioactivity of an expressed target protein is almost totally lost after denaturation and renaturation. The fusion with SUMO (Small ubiquitin-related modifier) and FGF21 by PCR was able to promote the soluble expression of the target protein (Wang et al. 2010; Yu et al. 2014). For the concern of large-scale production, fermentation in 30-L to 200-L scale was used to establish a time-saving and cost-effective strategy for industrial production of rhFGF21 (Ye et al. 2016; Hui et al. 2019; Ye et al. 2019). The successful expression of FGF21 in yeast, tomato, Arabidopsis, carrot, and rice has been achieved gradually (Song et al. 2016; Wang et al. 2016).