P144 peptide

P144 peptide

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

H-TSLDASIIWAMMQN-OH

H-Thr-Ser-Leu-Asp-Ala-Ser-Ile-Ile-Trp-Ala-Met-Met-Gln-Asn-OH

14

95.18%

C₆₈H₁₀₉N₁₇O₂₂S₂

1580.81

Synthetic

Powder

P144 (TSLDASIIWAMMQN), a hydrophobic peptide derived from the sequence of the extracellular region of type III receptor for TGF-β (Betaglycan, amino acids 730–743). P144 reduces early CNV progression in a laser-induced rat model. This is achieved through downregulation of VEGF and TGF-β, but also by affecting other mediators involved in the angiogenic process, such as COX-2, MMP-2 and MMP-9. P144 may have an antiangiogenic role in CNV treatment affecting the main target of current treatments through TGF-β inhibition.

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

• Zarranz-Ventura J, Fernández-Robredo P, Recalde S, Salinas-Alamán A, Borrás-Cuesta F, Dotor J, García-Layana A. Transforming growth factor-beta inhibition reduces progression of early choroidal neovascularization lesions in rats: P17 and P144 peptides. PLoS One. 2013 May 31;8(5):e65434. doi: 10.1371/journal.pone.0065434. PMID: 23741494; PMCID: PMC3669249.

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.