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Review
. 2022 Mar 12;23(6):3068.
doi: 10.3390/ijms23063068.

Vasopressin and Its Analogues: From Natural Hormones to Multitasking Peptides

Mladena Glavaš  1 , Agata Gitlin-Domagalska  1 , Dawid Dębowski  1 , Natalia Ptaszyńska  1 , Anna Łęgowska  1 , Krzysztof Rolka  1
Affiliations
Review

Vasopressin and Its Analogues: From Natural Hormones to Multitasking Peptides

Mladena Glavaš et al. Int J Mol Sci. .

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.

Keywords: desmopressin; vasoconstrictors; vasopressin; vasopressin analogues; vasopressin receptors.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Timeline for development of AVP peptide analogues [28,29,30,31,32,33,34,35].
Figure 2
Figure 2
Structures of (a) arginine vasopressin (AVP) and (b) oxytocin (OXT). Differences in sequence are shown in blue and red.
Figure 3
Figure 3
Schematic presentation of AVP receptors, their position and role in the body.
Figure 4
Figure 4
Non-peptide agonists and antagonists of AVP receptor.
Figure 5
Figure 5
Natural peptide analogues of AVP, (a) LVP and (b) phenypressin. Amino acids that are not present in AVP are shown in red.
Figure 6
Figure 6
Structure of peptide LVP analogues. The modifications are shown in blue and red. d = deamination of N-terminal Cys (Cys1); Dbt = 3,5-dibromo-l-tyrosine; Thi = thienilalanine; diHPhe = dihydrophenylalanine; Abu = 4-α-aminobutyric acid (AABA); Cha = 1-amino-cyclopentanecarboxylic acid (cyclohexylalanine); Eda = ethylendiamine.
Figure 7
Figure 7
Structures of selected synthetic peptide analogues of AVP. Modifications are shown in different colors. d = deamination of N-terminal cysteine (Cys1); diPhe = 3,3-diphenyl-l-alanine; d-diPhe = 3,3-diphenyl-d-alanine; l-1-Nal = l-1-napthylalanine; l-2-Nal = l-2-napthylalanine; Aic = 2-aminoindane-2-carboxylic acid; Apc = 1-aminocyclopentane-1-carboxylic acid; Sar= l-sarcosine; NMeAla= N-methyl-l-alanine; HNle = l-homonorleucine; HyLeu = l-hydroxynorleucine.
Figure 8
Figure 8
Synthetic peptide analogues of AVP. Modifications are shown in different colors. hGln = homoglutamine, Orn(i-Pr) = N-δ-iso-propyl-l-ornithine.
Figure 9
Figure 9
Analogues of dDAVP. Modifications are shown in different colors. Aic = 2-aminoindane-2-carboxylic acid; diPhe = 3,3-diphenyl-l-alanine; Thi = thienilalanine.
Figure 10
Figure 10
AVP receptor antagonists.
See this image and copyright information in PMC

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