China
Africa
Explore chapters and articles related to this topic
An Overview of Protease Inhibitors
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Veena Sreedharan, K.V. Bhaskara Rao
Proteases are seen in prokaryotes, fungi and animals and are very necessary for their survival. Proteases are enzymes that help to break down proteins in a method known as proteolysis. Such enzymes are present in a wide range of biological activities, from small protein digestion to extremely controlled cascades. Protease, like hormones, antibodies, and other enzymes, shows a vital physiological part in determining the life span of other proteins. In the physiology of organisms, this is one of the profligated “switching on” and “switching off” regulating systems. Proteases are secreted by a variety of bacteria to break the protein–peptide link into simple small monomers. As a result of multiple clinical trials suggesting their benefits in cancer studies include inflammations, immune regulations and blood flow control, their usage in medicine is garnering more and more attention. Many parasites are involved in pathogenesis, which includes parasite relocation through the host tissue barrier, hemoglobin and blood protein breakdown, immunological invasions, and inflammatory activation. Proteases thus show a decisive part in pathogenesis. Wild action, on the other hand, has negative consequences in the human body. These enzymes found within cancer cells have the ability to break other strong cell wall and membrane, allowing them to spread and grow into additional cell organ and part of the body, resulting in spread from one site to another (Figure 19.1).
*
Published in Valerio Voliani, Nanomaterials and Neoplasms, 2021
Xuan Yang, Miaoxin Yang, Pang Bo, Madeline Vara, Younan Xia
Proteases represent a major class of enzymes that catalyze the hydrolysis of peptide bonds to break down proteins into smaller pieces in a process known as proteolysis [407]. To this end, protein-stabilized fluorescent Au clusters can serve as probes for the detection of proteases. In the presence of proteases, the protein shell around each Au cluster will be broken down and the photoluminescence will be effectively quenched by the O2 from ambient air (Fig. 5.28A,B). By simply changing the protein substrates surrounding the Au clusters, this assay could be easily adapted for the detection of different proteases. With BSA-stabilized fluorescent Au clusters, the LOD for proteinase K reached 1 ng mL−1. Based on the selective interactions with ligands, many small molecules and heavy metal ions can also be detected through the principle of quenching photoluminescence from the Au clusters [415, 417].
Biophysical and Biochemical Characterization of Peptide, Protein, and Bioconjugate Products
Published in Sandeep Nema, John D. Ludwig, Parenteral Medications, 2019
Tapan K. Das, James A. Carroll
There are a variety of methods that are useful for detecting, characterizing, and quantifying charge variants in proteins [110]. These include IEF, capillary IEF, capillary zone electrophoresis [111], and ion exchange chromatography (IEC) [112]. The advantages of these methods are that they can separate and quantify overall charge heterogeneity. However, they give little or no information concerning the types or sites of charge heterogeneity present in the molecule. For monitoring stability, inherent charge variability may interfere with the ability to monitor degradation using these methods. An example is the assessment of deamidation in a glycoprotein in the presence of significant heterogeneity in sialic acid levels. So, while these methods may be appropriate for routine batch release and monitoring of consistency, more detailed characterization is required to gain information on the presence of specific modifications leading to charge heterogeneity. Site-specific information can be assessed using approaches involving proteolysis and LC/MS. This approach can be used to characterize and quantify, for example, deamidation at a specific site in the presence of inherent heterogeneity elsewhere in the molecule.
In vitro antioxidant activity evaluation of pine nut peptides (Pinus koraiensis) fermented by Bacillus subtilis LS-45
Published in Preparative Biochemistry & Biotechnology, 2023
Jiajia Sun, Zhi Zhang, Kexin Yang, Gang Wei, Yanxia Li
Consequently, pine nut protein is a fantastic source of protein. Recent advancement in the production and use of pine nuts (Pinus koraiensis) include the creation of pine nut milk beverage processing technology and a preliminary investigation of pine nut beverage preparation technology. However, pine nuts do not have a high protein utilization rate. Because pine nuts are eaten raw, the body cannot fully absorb their nutrients.[13,14] It will be easier for nutrients to be absorbed if large-molecule proteins are broken down into small-molecule peptides. Nowadays, enzymatic techniques for proteolysis, such as neutral protease, trypsin, alkaline protease, etc., are frequently used in academic settings. The rate of protein hydrolysis is low in some circumstances. Microorganisms may convert big molecular proteins into small molecular peptides through their physiological processes, and some researchers have generated protein peptides through microbial fermentation.[15] The protein peptides are produced by microbial fermentation, which makes them easier for the body to absorb and gives them a minimum cost and a milder taste.[16]
Comparative study of the nucleophilic attack step in the proteases catalytic activity: A theoretical study
Published in Molecular Physics, 2020
Sebastián A. Cuesta, José R. Mora, Cesar H. Zambrano, F. Javier Torres, Luis Rincón
Proteolysis is a biochemical process in which proteins are split in shorter amino-acid chains by means of the cleavage of their peptide bonds [1–3]. This process is considered fundamental for biological systems, due to its key regulatory function involving metabolism, organelle shaping, pathogenicity, release of membrane-tethered protein domains, among others [3]. It is well-known that the uncatalysed proteolysis is very demanding from the energetic point of view [4]; therefore, in nature, this reaction occurs in the presence of proteases enzymes (also known as peptidases or proteinases). This family of enzymes can be found in any life domains and due to its importance in the replication process of living cells; they have been the object of intensive research during the last decade [5–11]. In this regard, the reaction mechanism involving proteases has been studied to gain insights in the inhibition of different types of parasitic and viral infections, which subsequently may be used for the design and development of highly specific antivirals [1–3,12].
New approaches towards the discovery and evaluation of bioactive peptides from natural resources
Published in Critical Reviews in Environmental Science and Technology, 2020
Nam Joo Kang, Hyeon-Su Jin, Sung-Eun Lee, Hyun Jung Kim, Hong Koh, Dong-Woo Lee
Peptides generated by enzymatic proteolysis perform many vital functions in biological metabolism and signaling. Over 60 linear and cyclized peptides with pharmaceutical activities, such as insulin, adrenocorticotropic hormone, calcitonin, oxytocin, vasopressin, and octreotide, are currently used as anti-cancer, anti-obesity, and immunomodulatory agents (Lau & Dunn, 2018). When used over prolonged periods, however, small molecules as synthetic drugs are not free from side effects, suggesting that natural compounds and their derivatives represent safer alternatives for therapeutic applications (Dimopoulos et al., 2014). In light of this, BPs derived from natural resources such as foods and plants are ranked above small molecules in terms of biosafety (Lau & Dunn, 2018). From an industrial standpoint, natural BPs have segmented the peptide therapeutics market according to application (food vs. pharmacological), source, manufacturer, route of administration, synthesis technology, and region. In particular, the source of origin (i.e. animal vs. plant) and type of manufacturing processes (chemical vs. biological) are critical determinants of contemporary customers’ preferences in the food and pharmaceutical industries (Tucker et al., 2016).