NT-1 peptide

NT-1 peptide

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

Batch to batch variation of the purity

H-TLWPFDLWLKTR-OH

H-Thr-Leu-Trp-Pro-Phe-Asp-Leu-Trp-Leu-Lys-Thr-Arg-OH

12

95.86%

C₇₈H₁₁₄N₁₈O₁₇

1575.84

Synthetic

Powder

NT-1 at extremely low concentration (3 nM) in solutions could be efficiently captured by immobilized sTNP(standard tyrosine-nitrated peptide) as determined by pull-down and subsequent MALDI-TOF MS analysis. Surface plasmon resonance (SPR) measurement confirmed that NT-1 possesseed a good selectivity, showing more than 100-fold higher binding affinity with TNP than its non-nitrated counterpart. Moreover, NT-1 could efficiently capture various types of TNPs in solutions even in the presence of 1000-fold excessive amount of trypsinized BSA fragments. Most importantly, NT-1 showed superiority to commercially used nitrotyrosine antibody as the former captured more TNPs, with less sequence preference.

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

• Cheng Y, Qi J, Liu K, Zhou C, Wang W, Zuo Y, Zhang P, Liang S, Wang Y, Chen P, Tang C, Liu Z. Characterization of a novel affinity binding ligand for tyrosine nitrated peptides from a phage-displayed peptide library. Talanta. 2022 May 1;241:123225. doi: 10.1016/j.talanta.2022.123225. Epub 2022 Jan 13. PMID: 35066280.

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.