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An Overview of Protease Inhibitors
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Veena Sreedharan, K.V. Bhaskara Rao
Proteases, a vast family of enzymes involved in a wide range of physiological processes, have been identified as prospective therapeutic targets (McKerrow et al., 2006). Increased proteolysis has been demonstrated to accentuate a variety of disease processes, making proteases chief therapeutic targets (Turk, 2006; Drag and Salvesen, 2010; Santos, 2009; Sabotic and Kos, 2012). Management of hypertension with angiotensin-converting-enzyme (ACE) inhibitors, AIDS treatment developed with HIV protease inhibitors, and multiple myeloma treatment with protein complex inhibitors are all examples of effective PIs utilized in the therapeutic involvement of numerous illnesses. The development of chemicals that specifically inhibit enzymes that are critical for the survival of parasites inside the host and are part of parasites’ metabolic processes is one prospective technique for treating parasitic disorders (Figure 19.2). Because of their functions in replication, metabolism, existence, and sickness, site proteases are interesting targets (Selzer et al., 1997).
Pharmaceuticals and Nutraceuticals from Fish Wastes and Their Activities
Published in Ramasamy Santhanam, Santhanam Ramesh, Subramanian Nivedhitha, Subbiah Balasundari, Pharmaceuticals and Nutraceuticals from Fish and Fish Wastes, 2022
Ramasamy Santhanam, Santhanam Ramesh, Subramanian Nivedhitha, Subbiah Balasundari
Enzymatic hydrolysis: This process is carried out with proteolytic enzymes, namely, endopeptidases and exopeptidases. Production of FPH is largely influenced by many factors, such as the composition of raw material, type of enzyme used, hydrolysis conditions, and degree of hydrolysis (DH).
Envisioning Utilization of Super Grains for Healthcare
Published in Megh R. Goyal, Preeti Birwal, Santosh K. Mishra, Phytochemicals and Medicinal Plants in Food Design, 2022
Proteolytic enzymes play an important in the human body as they are responsible for the metabolism of the proteins. Antinutritional factors like protease inhibitors form undesirable complexes with such enzymes which hinder their activity. In gastrointestinal tract, the complexation of protease inhibitors with trypsin reduces the metabolic activity of the enzyme, thus the pancreases produce more enzymes leading to pancreatic hypertrophy and consequently growth reduction (Tables 10.2 and 10.3). However, these antinutritional factors can be easily destroyed through domestic cooking which is attributed to their thermolabile nature [97, 107]. Super grains like quinoa contain very low levels of protease inhibitors, that is, 1.36–5.04 unit trypsin inhibitor (TIU) per mg, which makes them highly digestible [187] as compared to the lentils (17.8 TIU per mg), soybean (24.5–41.5 TIU per mg) and beans (12.9–42.8 TIU per mg) [87].
Subcutaneous catabolism of peptide therapeutics: bioanalytical approaches and ADME considerations
Published in Xenobiotica, 2022
Simone Esposito, Laura Orsatti, Vincenzo Pucci
The most relevant biotransformation occurring at the SC injection site is the cleavage of peptide bonds by means of proteases or peptidases, which generates smaller peptides or amino acids. This type of biotransformation is referred to as catabolism, in contrast to the term metabolism used for biotransformation mainly observed in small molecules. Proteolytic enzymes are broadly divided into two categories: exopeptidases, which catalyse the cleavage at the N-terminal or C-terminal removing a single amino acid, and endopeptidases, which cleave peptide bonds within the sequence (López-Otín and Bond 2008). Exopeptidases are intuitively divided into aminopeptidases and carboxypeptidases, while endopeptidases are traditionally classified on the basis of their catalytic site as cysteine peptidases (e.g. dipeptidyl peptidase IV), aspartic peptidases (e.g. pepsin), serine peptidases (e.g. cathepsin B), and metallopeptidases (e.g. matrix metalloprotease 2 and 9) (de Veer et al. 2014a).
Establishing molecular signatures of stroke focusing on omic approaches: a narrative review
Published in International Journal of Neuroscience, 2020
Abhilash Ludhiadch, Kanika Vasudeva, Anjana Munshi
Proteomics, a complex field of study in molecular biology, is concerned with systematic high throughput analysis of protein expression of a particular cell type or an organism. The study focuses on the final gene product rather than the gene itself, and also involves post translational modifications of proteins. Proteomic studies have gained momentum on the account of technological advances such as mass spectrometry equipped with LC–MS-MS, MALDI-TOF/TOF and bioinformatics tools [65,66]. It not only helps the other ‘omics’ technologies such as genomics and transcriptomics to delineate the individuality of proteins of an organism, but also to perceive the function and structure of a specific protein. The human proteome contains many thousand peptides that are broken down parts from larger proteins by the activity of endogenous proteolytic enzymes. The latter consists the peptidome. The comparison of proteome or peptidome profiles of patients and controls can thus be used for finding new biomarkers for the diagnosis, prognosis and treatment measures in complex diseases including stroke [67]. Proteomics technologies are used in stroke for various research settings such as alteration of expression patterns of specific protein in response to different signals, detection of various diagnostic markers, and interpretation of functional protein pathways during treatment processes [66,68].
Research progress on therapeutic targeting of quiescent cancer cells
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2019
Jinhua Zhang, Jing Si, Lu Gan, Cuixia Di, Yi Xie, Chao Sun, Hongyan Li, Menghuan Guo, Hong Zhang
Proteasome inhibitors are capable of blocking the proteolytic activity of the proteasome complex. Inhibition of proteasomes exerts several toxic effects, including accumulation of unfolded and damaged proteins as well as elevated ROS levels [5]. In small-cell lung cancer, two proteasome inhibitors, bortezomib and siomycin A, successfully suppressed Forkhead box protein M1 (FOXM1) and NF-κB activity, resulting in significant cell cycle arrest and apoptosis induction in line with reduced cell proliferation. In particular, these effects were further strengthened by the supplementation of conventional chemotherapy with bortezomib [61]. Administration of 5-azacytidine combined with bortezomib in multiple myeloma (MM) may present a novel therapeutic strategy to delay recurrence by potentiating bortezomib-mediated apoptosis and quiescence stability [62]. Therefore, integration of proteasome inhibitors into conventional therapeutic strategies may present a promising approach for the treatment of multiple cancer types.