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.
Finding a Target
Nathan Keighley in Miraculous Medicines and the Chemistry of Drug Design, 2020
The instructions for producing proteins are encoded on genes, sections of DNA, which are transcribed on to RNA before being translated into a protein chain at ribosomes; cell organelles designed for this operation. This is a very intricate enzyme-controlled biological pathway, with a high degree of complexity. Proteins produced from this process then adopt their specific three-dimensional shape and move to their intended location to perform a given function in the body. Nucleotide triplets code for particular amino acids; the order in which these triplets are assembled in the gene determines the sequence of amino acids in the protein and therefore ultimately governs the proteins shape and function. The different side chains of each of the 20 amino acids can form a variety of hydrogen bonds; hence the observed variety of possible structures. Proteins are very versatile molecules that can have many functions, governed by their structural organisation. For globular proteins such as those involved in catalysis and molecular recognition, the final folded three-dimensional shape of a polypeptide, the tertiary structure, may constitute one protein domain, and several globular units comprise the functional quaternary structure, as with haemoglobin. In order for polypeptides to assemble into a functioning quaternary structure, precise interactions between these molecules must be in place.
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
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].
Application of plant-derived exosome-like nanoparticles in drug delivery
Published in Pharmaceutical Development and Technology, 2023
Mohadeseh Barzin, Amir Mohammad Bagheri, Mandana Ohadi, Amir Masoud Abhaji, Soodeh Salarpour, Gholamreza Dehghannoudeh
Proteins are macro-biomolecules composed of amino acid residues and perform a wide variety of functions, including DNA replication, stimuli responding, transferring molecules, and catalyzing metabolic reactions (Whitford 2013; Fuxreiter and Vendruscolo 2021). Suharta et al. (2021) revealed that PELNs have a low concentration of protein; Further, most proteins in PELNs are cytosolic proteins, including proteases, actin, and membrane proteins that act as transporters within the membrane. However, determining a complete protein profile inside PELNs is challenging due to various sets of protein databases in different plants (Suharta et al. 2021; Woith et al. 2021). For instance, Ju et al. (2013) identified 580 proteins of lemon-derived exosomes. On the other hand, compared to exosomes extracted from animal cells, PELNs have lower protein content. Somehow, mammalian-derived exosomes contain more than 1000 proteins, whereas plant exosomes derived from ginger have only 28 proteins (Raimondo et al. 2015; Zhang et al. 2016; Salek et al. 2020; Suharta et al. 2021). Moreover, it should be noted that proteins are assumed to play a critical role in interspecies recognition within the plant and mammalian cells (Song et al. 2020; Nemati et al. 2022). For example, lectin proteins, which have a high specific affinity for saccharides and are abundantly found in some plant-derived exosomes such as garlic and mushrooms, are supposed to be the primary interspecies communication mediators between these exosomes and mammalian cells (Song et al. 2020).
The development of peptide- and oligonucleotide-based drugs to prevent the formation of abnormal tau in tauopathies
Published in Expert Opinion on Drug Discovery, 2023
Madia Lozupone, Vittorio Dibello, Rodolfo Sardone, Fabio Castellana, Roberta Zupo, Luisa Lampignano, Ilaria Bortone, Roberta Stallone, Mario Altamura, Antonello Bellomo, Antonio Daniele, Vincenzo Solfrizzi, Francesco Panza
Between small molecules and proteins, peptides are a particular class of pharmaceutical compounds. Proteins are huge biomolecular constituted by one or more long chains of amino acid residues. Proteins are important regulators of biological functions including the transport of chemicals, giving a structure to cells and organisms, the response to stimuli, replication of DNA, and a catalysis of metabolic reactions. Peptides, with high biological activity, selectivity, and low toxicity, can be created by the enzymatic protein digestion, have often fewer than 20–30 amino acid residues, and represent a viable alternative to chemical compounds. In vivo, unfortunately, peptide medicines have short half-life and proteases generally rapidly destroyed these compounds. This factor can substantially impedes their clinical development, constituting challenges for administration and transport, in particular to the brain [77].
Related Knowledge Centers
- Biomolecule
- Cell Signaling
- Cytoskeleton
- DNA Replication
- Enzyme Catalysis
- Fibrous Protein
- Intracellular Transport
- Macromolecule
- Residue
- Amino Acid
- DNA Replication