Therapeutic peptides are a promising frontier in precise medicine, leveraging unique properties for targeted treatment. Advancements in production, modification, and delivery have surmounted challenges. Originating from human hormones and natural sources, peptides hold potential for various conditions, including cardiovascular diseases. They offer a transformative approach for tailored, effective medical interventions.
In the ever-evolving landscape of modern medicine, therapeutic peptides have emerged as a promising avenue for targeted and precise treatment. These short chains of amino acids hold immense potential due to their distinctive properties and mechanisms of action. The production and modification of peptides[1] have been achieved using both chemical and biological methods, along with new design and delivery strategies. This has enabled peptides to overcome their inherent disadvantages and continue to progress.
What are Therapeutic Peptides?
Therapeutic peptides represent a distinct category of pharmaceutical agents composed of meticulously arranged amino acids, often weighing between 500 and 5000 Da. The journey into researching therapeutic peptides[2] commenced with foundational investigations into natural human hormones—such as insulin, oxytocin, vasopressin, and gonadotropin-releasing hormone (GnRH)—and their specific physiological functions within the human body.
Since the inaugural synthesis of insulin, the first therapeutic peptide, in 1921, notable advancements have been achieved, leading to the approval of over 80 peptide drugs worldwide. This evolution in peptide drug development has established itself as a prominent subject within pharmaceutical research.
Peptides Found From Living Organisms
Bioactive peptides produced by bacteria, fungi, plants, and animals are capable of exhibiting therapeutic properties. VEGF-F and svVEGF, for example, are analogues of vascular endothelial growth factor (VEGF) found in snake venom. The cyclic peptides, which are rich in disulfide bonds and often have fewer than 80 residues, are responsible for cytotoxicity by targeting ion channels and membrane receptors. In recent years, venom peptides have been adapted for therapeutic purposes, such as exenatide, which is derived from Gila monster venom. A peptide derived from Conus magus venom, ziconotide, has also shown promise in treating chronic neuropathic pain.
Therapeutic Peptides in Cardiovascular Disease Treatment
Globally, cardiovascular disease ranks first among non-communicable diseases in terms of mortality and morbidity. Hypertension, a primary risk factor for cardiovascular disease, arises from heightened activity of the renin-angiotensin-aldosterone system (RAAS) and the sympathetic nervous system, coupled with sodium retention. The pivotal role of angiotensin-converting enzyme (ACE) in RAAS involves cleaving angiotensin I into angiotensin II, inducing vasoconstriction and indirectly elevating blood pressure.
Conversely, ACE2 hydrolyzes angiotensin II into vasodilator angiotensin (1-7), contributing to blood pressure reduction. Manipulating RAAS emerges as an optimal strategy for cardiovascular disease control.
FDA-approved synthetic angiotensin II, introduced in 2017, increases blood pressure via intravenous infusion for adults with septicemia or distributed shock. Noteworthy peptides identified from Tetradesmus obliquus microalgae by Montone et al. exhibit ACE inhibitory activity.
Liao et al. revealed that the tripeptide IRW, sourced from egg white, lowered blood pressure in spontaneously hypertensive rats by up-regulating ACE2 expression. These investigations underscore the potential of food-derived peptides targeting RAAS as a promising avenue for cardiovascular disease treatment.
Summary
Therapeutic peptides represent a revolutionary approach to precision medicine, offering tailored treatments with minimal side effects. As research progresses, therapeutic peptides are poised to play an increasingly pivotal role in shaping the landscape of medical interventions, ultimately improving patient outcomes and advancing the frontiers of medicine.
References:
Henninot, A., Collins, J. C. & Nuss, J. M. The current state of peptide drug discovery: back to the future? J. Med Chem. 61, 1382–1414 (2018).
Goodfriend, T. L. & Calhoun, D. A. Resistant hypertension, obesity, sleep apnea, and aldosterone: theory and therapy. Hypertension 43, 518–524 (2004).
Simoes, E. S. A. C. & Teixeira, M. M. ACE inhibition, ACE2 and angiotensin-(1-7) axis in kidney and cardiac inflammation and fibrosis. Pharm. Res 107, 154–162 (2016)
Correa, T. D., Takala, J. & Jakob, S. M. Angiotensin II in septic shock. Crit. Care 19, 98 (2015).
Montone, C. M. et al. Peptidomic strategy for purification and identification of potential ACE-inhibitory and antioxidant peptides in Tetradesmus obliquus microalgae. Anal. Bioanal. Chem. 410, 3573–3586 (2018).
Liao, W., Fan, H., Davidge, S. T. & Wu, J. Egg white-derived antihypertensive peptide IRW (Ile-Arg-Trp) reduces blood pressure in spontaneously hypertensive rats via the ACE2/Ang (1-7)/Mas receptor axis. Mol. Nutr. Food Res 63, e1900063 (2019).
Footnotes:
1. https://kactusbio.com/products/human-hla-e-01-03-complex-protein-mhc-hm406
2. https://kactusbio.com/pages/mhc-complexes
Rienzi Mosqueda is a dedicated writer specialising in life science, health, and pharma content. With a passion for clear, engaging writing, Rienzi provides fresh perspectives on each topic. His ability to simplify complex ideas makes the articles valuable for readers of all backgrounds. As an emerging voice, Rienzi Mosqueda is committed to sharing knowledge and sparking discussions through their impactful writing.
