APGWamide, >98% purity peptide (TFA removed)

APGWamide, >98% purity peptide (TFA removed)

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

APGW

H-Ala-Pro-Gly-Trp-NH2

4

98.99%

C₂₁H₂₈N₆O₄

428.5

50064302

Synthetic

Powder

APGWamide was found in ferrugineus spindle (Fusinus ferrugineus), freshwater great pond snail (Lymnaea stagnalis), octopus (Octopus vulgaris).
APGWamide is a neuropeptide believed to be the Penis Morphogenic Factor (PMF) responsible for the initial growth of male accessory sex organs (ASO) in gastropods, maintained by androgenic steroids through a positive feedback loop.
APGWamide is highly conserved among mollusks and plays a crucial role in mating behavior, myogenic activity, and growth of ASO in imposex gastropods after exposure to tributyltin (TBT).
As for application, it is proposed that APGWamide can control the growth of imposex structures and may be the PMF responsible for this phenomenon. APGWamide induces imposex to the same extent as TBT or testosterone (T), with a threshold dose near 10^(-16) moles.
Conopressin and APGWGNamide can act as antagonist to APGWamide.

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

• Kuroki Y, Kanda T, Kubota I, et al. A molluscan neuropeptide related to the crustacean hormone, RPCH. Biochem Biophys Res Commun. 1990;167(1):273-9.
• Oberdörster E, McClellan-Green P. The neuropeptide APGWamide induces imposex in the mud snail, Ilyanassa obsoleta. Peptides. 2000 Sep;21(9):1323-30.
• Ohtani M, Minakata H, Aimoto S. Potent antagonistic action of synthetic analogues of APGWGNamide, an antagonist of molluscan neuropeptide APGWamide. Peptides. 2002 May;23(5):843-52.
• Tait CC, Olson MN, Nedeljkovic K, Kirchner E, Katz PS. Expression patterns and behavioral effects of conopressin and APGWamide in the nudibranch Berghia stephanieae. Peptides. 2024;179:171253. doi:10.1016/j.peptides.2024.171253

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.