Abstract
Human neurohormone vasopressin (AVP) is synthesized in overlapping regions in the hypothalamus. It is mainly known for its vasoconstricting abilities, and it is responsible for the regulation of plasma osmolality by maintaining fluid homeostasis. Over years, many attempts have been made to modify this hormone and find AVP analogues with different pharmacological profiles that could overcome its limitations. Non-peptide AVP analogues with low molecular weight presented good affinity to AVP receptors. Natural peptide counterparts, found in animals, are successfully applied as therapeutics; for instance, lypressin used in treatment of diabetes insipidus. Synthetic peptide analogues compensate for the shortcomings of AVP. Desmopressin is more resistant to proteolysis and presents mainly antidiuretic effects, while terlipressin is a long-acting AVP analogue and a drug recommended in the treatment of varicose bleeding in patients with liver cirrhosis. Recently published results on diverse applications of AVP analogues in medicinal practice, including potential lypressin, terlipressin and ornipressin in the treatment of SARS-CoV-2, are discussed.
Highlights
Homeostasis of living organisms requires continuous and strict regulation
Vasopressin is a nonapeptide comprising a tripeptide tail and a cyclic structure formed by six residues with a disulfide bridge between cysteines at positions 1 and 6 [36–38]
The results showed that LVP stimulating adrenocorticotropic hormone (ACTH) secretion in BIPSS test for Cushing’s syndrome (CS) and 10 units LVP correctly lateralized the pituitary adenoma in threefourths of patients
Summary
Homeostasis of living organisms requires continuous and strict regulation. The management of all body functions involves various mechanisms and components that need to be efficiently coordinated. Peptides occur naturally and are usually considered to be safer than synthetic drugs They are more selective and specific and, what is important, they are degraded into nontoxic metabolites (amino acids) [14,15]. Taking it all into account, the introduction of peptides as drugs should be easy to handle Despite their involvement in various bioactivities in living organisms and quite extensive knowledge regarding synthesis and structure–activity relationships, the. For this ties make them extremely attractive candidates to become therapeutics For this reason, reason, modifications of peptide‐based drug candidates increasing their metabolic modifications of peptide-based drug candidates increasing their metabolic stability and stability and bioavailability, and retaining their functions are of high demand.
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