Enhancing Stability and Bioavailability of Peptidylglycine Alpha-Amidating Monooxygenase in Circulation for Clinical Use.

ABSTRACT: Peptidylglycine alpha-amidating monooxygenase (PAM) is the only enzyme known to catalyze C-terminal amidation, a final post-translational modification step essential for the biological activity of over 70 bioactive peptides, including adrenomedullin (ADM), calcitonin gene-related peptide (CGRP), amylin, neuropeptide Y (NPY), and others. Bioactive (amidated) peptide hormones play crucial roles in various physiological processes and have been extensively explored as therapeutic compounds in clinical and preclinical research. However, their therapeutic viability is limited due to their short half-life and, in most cases, the need for prolonged infusion to maintain effective concentrations. PAM itself has also been considered as a therapeutic compound aiming to increase the level of amidated p

SUBMITTER: Ilina Y 

PROVIDER: S-EPMC11853079 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature