Short communicationComparison of responses to adrenomedullin and adrenomedullin analogs in the mesenteric vascular bed of the cat
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Adrenomedullin – Current perspective on a peptide hormone with significant therapeutic potential
2020, PeptidesCitation Excerpt :The activation motif of the CT/CGRP family peptide hormones consists of the disulfide-bonded ring structure and a C-terminally adjacent helix. While the motif is located at the very N-terminus of α/β-CGRP, AMY and CT, the peptide hormones ADM and IMD contain beforementioned N-terminal extensions, which can be truncated without any loss of activity [8,9,11,12,33]. Furthermore, it was recently reported that the deletion of the ADM DKDKD interdomain section ([Δ35−39]ADM15−52) results in a significant increase of efficacy but reduced potency of approximately 100-fold.
Natural and synthetic peptides in the cardiovascular diseases: An update on diagnostic and therapeutic potentials
2019, Archives of Biochemistry and BiophysicsCitation Excerpt :Peptides without the C terminal Tyr 52 or the C-terminal amide (AM 1–51, AM 1-51-OH, and AM 1-52-OH) showed much weaker binding than full-length AM [258,259], suggesting the important role of Tyr-NH2 in high affinity binding (see Table 3). N-terminally truncated peptides retaining the cyclic ring structure, such as AM 13–52, AM 15–52 or AM 16–52, exhibit similar binding efficacies [258,259] and vasodilatory effects as full-length AM [260–262] (Table 3). Furthermore, a linearized analogue with methylcarbamoyl esters (CAM) at both cysteines [[Cys[CAM]16,21] AM [1–52] revealed a decrease in binding and a loss of activation potency at the AM1 receptor, suggesting a key role of the disulfide-bridge for receptor activation [258].
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