Neuropeptide Y

Neuropeptide Y

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

YPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRY

Tyr-Pro-Ser-Lys-Pro-Asp-Asn-Pro-Gly-Glu-Asp-Ala-Pro-Ala-Glu-Asp-Met-Ala-Arg-Tyr-Tyr-Ser-Ala-Leu-Arg-His-Tyr-Ile-Asn-Leu-Ile-Thr-Arg-Gln-Arg-Tyr

36

97.5%

C₁₈₉H₂₈₅N₅₅O₅₇S

4271.5

Synthetic

Powder

N-terminal truncation enhances peptide antimicrobial activity. It showed a moderate activity against E. coli ATCC 25922 (MIC 46.5 ug/ml) and very weak activity against S. mutans NCTC 10449, L acidophilus NCTC 1723, E. faecalis NCTC 12697, P. aeruginosa ATCC 27853, and C. albicans NCTC 3179 (MIC 125-280 ug/ml). 3D structure was determined at pH 3.2 and 37oC by 2D NMR. Residues 13-36 form a well-defined amphipathic helix. Dimers co-exist in the NMR solution. You can rotate, zoom, and view the 3D structure here in the PDB. Updated 5/2014; Jan2015. Neuropeptide Y has Antifungal activity. The source of Neuropeptide Y is brain, Homo sapiens.

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

• Minth CD, Bloom SR, Polak JM, Dixon JE. Cloning, characterization, and DNA sequence of a human cDNA encoding neuropeptide tyrosine. Proc Natl Acad Sci USA. 1984;81(14):4577-81.

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.