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Structural Features Influencing the Bioactive Conformation of Angiotensin II and Angiotensin A: Relationship between Receptor Desensitization, Addiction, and the Blood-Brain Barrier

The N-terminal portion of the octapeptide angiotensin II (DRVYIHPF; AngII), a vasopressor peptide that favorably binds to, and activates, AngII type 1 receptor (AT R), has an important role in maintaining bioactive conformation. It involves all three charged groups, namely (i) the N-terminal amino g...

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Bibliographic Details
Published in:International journal of molecular sciences 2024-06, Vol.25 (11), p.5779
Main Authors: Moore, Graham J, Ridway, Harry, Gadanec, Laura Kate, Apostolopoulos, Vasso, Zulli, Anthony, Swiderski, Jordan, Kelaidonis, Konstantinos, Vidali, Veroniki P, Matsoukas, Minos-Timotheos, Chasapis, Christos T, Matsoukas, John M
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Language:English
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Summary:The N-terminal portion of the octapeptide angiotensin II (DRVYIHPF; AngII), a vasopressor peptide that favorably binds to, and activates, AngII type 1 receptor (AT R), has an important role in maintaining bioactive conformation. It involves all three charged groups, namely (i) the N-terminal amino group cation, (ii) the Asp sidechain anion and (iii) the Arg guanidino cation. Neutralization of any one of these three charged groups results in a substantial reduction (
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms25115779