On a commercial level, there are several peptide drugs that have reached blockbuster status. The study found that the average number of new peptide candidates entering clinical development in the 1970s was 1.2 per year, which rose to 4.6 per year in the 1980s, 9.7 per year in the 1990s, and 16.8 per year through 2000–2008 (1, 4). Although peptides represent a small portion of total drug candidates, the number of peptide drugs entering clinical development has increased during the past several decades, according to the Peptide Therapeutics Foundation analysis, which excluded insulins (1, 4). During 2000–2008, 60% of peptides entering clinical development targeted GPCRs, and most had agonist activity. The most common extracellular targets were G-protein coupled receptors (GPCRs), which include nearly 1000 transmembrane proteins that activate cellular response. The majority of peptide candidates target extracellular molecules with less than 10% binding to intracellular targets, according to an analysis of the peptide drug pipeline by the Peptide Therapeutics Foundation (1, 4). Patricia Van Arnum Although peptides have the size and functionality to effectively modulate intracellular protein–protein interactions, they often do not permeate cells and, therefore, are used to modulate extracellular targets such as receptors (1–3). These alpha-helical peptides have structural and functional properties that enable them to penetrate into the cell, bind to the therapeutic target, and modulate biological pathways. Stapled peptides, small modified helical proteins, are an emerging class of peptides that seek to address these limitations. Advancing Peptide Synthesis Through Stapled Peptides (SHUNYU FAN/GETTY IMAGES)Ěs a drug type, peptides offer certain benefits, such as specificity and potency, but they also present challenges, such as poor stability and short half-life.
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