Elabela(19-32)/ELA-14 (human) peptide

Elabela(19-32)/ELA-14 (human) peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

Pyr-RRCMPLHSRVPFP-OH

Pyr-Arg-Arg-Cys-Met-Pro-Leu-His-Ser-Arg-Val-Pro-Phe-Pro-OH

14

95.96%

C₇₅H₁₁₉N₂₅O₁₇S₂

1707.03

1886973-05-2

127043902

Synthetic

Powder

ELA(19-32) is a peptide fragment derived from the endogenous ligand of the apelin receptor (APJ), ELABELA (ELA). It is composed of the amino acid sequence Pyr-RR-C-M-P-L-H-S-R-V-P-F-P and was identified through the study of the structure-activity relationship of ELA. ELA(19-32) binds to APJ with a binding affinity in the nanomolar range and activates the Gα₁₁ and β-arrestin-2 signaling pathways, similar to the parent peptide ELA and the endogenous ligand apelin-13. It induces receptor internalization, although it is slightly less potent than apelin-13 and ELA in this regard. An alanine scan revealed that the C-terminal residues (Arg28, Val29, Pro30, Phe31, Pro32) and His26 are critical for binding and signaling. Replacements of these residues with alanine led to significant decreases in binding affinity and signaling potency. Additionally, replacements of N-terminal Arg20 and Arg21 only slightly decreased affinity. Both ELA and ELA(19-32) have been shown to cause hypotensive effects and enhance left ventricular contractility in ex vivo isolated-perfused heart and in vivo blood pressure and echocardiographic measurements.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual:Handling and Storage of Synthetic Peptides

• Murza A, Sainsily X, Coquerel D, Côté J, Marx P, Besserer-Offroy É, Longpré JM, Lainé J, Reversade B, Salvail D, Leduc R, Dumaine R, Lesur O, Auger-Messier M, Sarret P, Marsault É. Discovery and Structure-Activity Relationship of a Bioactive Fragment of ELABELA that Modulates Vascular and Cardiac Functions. J Med Chem. 2016 Apr 14;59(7):2962-72. doi: 10.1021/acs.jmedchem.5b01549. Epub 2016 Mar 30. PMID: 26986036.

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.