ATN 161 peptide

ATN 161 peptide

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

Batch to batch variation of the purity

Ac-PHSCN-NH2

Ac-Pro-His-Ser-Cys-Asn-NH2

5

95.87%

C₂₃H₃₅N₉O₈S

597.64

Synthetic

Powder

ATN 161 is a α5β1 integrin receptor antagonist that also binds to several other integrins, including α5β1 and αvβ3. ATN 161 is a 5-mer capped peptide derived from the synergy region (PHSRN) of human fibronectin, in which a cysteine residue replaces an arginine in the original sequence (PHSCN). ATN 161 has been shown to inhibit tumour growth, angiogenesis and metastasis and extend survival in multiple animal tumours, it has also shown activity outside oncology and can regress established Crohn's disease in several animal models.

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

• Livant et al (2000) Anti-invasive, antitumorigenic, and antimetastatic activities of the PHSCN sequence in prostate carcinoma. Cancer Res. 60 309 PMID: 10667582
• Khalili et al (2006) A non-RGD-based integrin binding peptide (ATN-161) blocks breast cancer growth and metastasis in vivo. Mol.Cancer Ther. 5 2271 PMID: 16985061
• Doñate (2008) Pharmacology of the novel antiangiogenic peptide ATN-161 (Ac-PHSCN-NH2): observation of a U-shaped dose-response curve in several preclinical models of angiogenesis and tumor growth. Clin Cancer Res. 14(7) 2137 PMID: 18381955

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.