p-Glu-Arg-Pro-Arg-Leu-Ser-His-Lys-Gly-Pro-Met-Pro-Phe and Hypotension

p-Glu-Arg-Pro-Arg-Leu-Ser-His-Lys-Gly-Pro-Met-Pro-Phe has been researched along with Hypotension* in 1 studies

Other Studies

1 other study(ies) available for p-Glu-Arg-Pro-Arg-Leu-Ser-His-Lys-Gly-Pro-Met-Pro-Phe and Hypotension

Article	Year
C-Terminal modifications of apelin-13 significantly change ligand binding, receptor signaling, and hypotensive action. Journal of medicinal chemistry, 2015, Mar-12, Volume: 58, Issue:5 Apelin is the endogenous ligand of the APJ receptor, a member of the G protein-coupled receptor family. This system plays an important role in the regulation of blood pressure and cardiovascular functions. To better understand the role of its C-terminal Phe(13) residue on ligand binding, receptor signaling, and hypotension, we report a series of modified analogues in which Phe(13) was substituted by unnatural amino acids. These modifications delivered new compounds exhibiting higher affinity and potency to inhibit cAMP accumulation compared to apelin-13. In particular, analogues Bpa(13) or (α-Me)Phe(13) were 30-fold more potent to inhibit cAMP accumulation than apelin-13. Tyr(OBn)(13) substitution led to a 60-fold improvement in binding affinity and induced stronger and more sustained drop in blood pressure compared to apelin-13. Our study identified new potent analogues of apelin-13, which represent valuable probes to better understand its structure-function relationship. Topics: Amino Acid Substitution; Animals; Apelin; Blood Pressure; Cyclic AMP; Hypotension; Intercellular Signaling Peptides and Proteins; Ligands; Male; Rats; Rats, Sprague-Dawley; Receptors, G-Protein-Coupled; Signal Transduction; Structure-Activity Relationship	2015

Article

Year

C-Terminal modifications of apelin-13 significantly change ligand binding, receptor signaling, and hypotensive action.

Journal of medicinal chemistry, 2015, Mar-12, Volume: 58, Issue:5

Apelin is the endogenous ligand of the APJ receptor, a member of the G protein-coupled receptor family. This system plays an important role in the regulation of blood pressure and cardiovascular functions. To better understand the role of its C-terminal Phe(13) residue on ligand binding, receptor signaling, and hypotension, we report a series of modified analogues in which Phe(13) was substituted by unnatural amino acids. These modifications delivered new compounds exhibiting higher affinity and potency to inhibit cAMP accumulation compared to apelin-13. In particular, analogues Bpa(13) or (α-Me)Phe(13) were 30-fold more potent to inhibit cAMP accumulation than apelin-13. Tyr(OBn)(13) substitution led to a 60-fold improvement in binding affinity and induced stronger and more sustained drop in blood pressure compared to apelin-13. Our study identified new potent analogues of apelin-13, which represent valuable probes to better understand its structure-function relationship.

Topics: Amino Acid Substitution; Animals; Apelin; Blood Pressure; Cyclic AMP; Hypotension; Intercellular Signaling Peptides and Proteins; Ligands; Male; Rats; Rats, Sprague-Dawley; Receptors, G-Protein-Coupled; Signal Transduction; Structure-Activity Relationship

2015