Shuchin 4 peptide

Shuchin 4 peptide

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

H-KAYSTPRCKGLFRALMCWL-NH2

H-Lys-Ala-Tyr-Ser-Thr-Pro-Arg-Cys-Lys-Gly-Leu-Phe-Arg-Ala-Leu-Met-Cys-Trp-Leu-NH2

19

95.66%

C₁₀₂H₁₆₃N₂₉O₂₂S₃

2243.75

Synthetic

Powder

Shuchin 4 is a peptide that was identified from the skin of the frog Rana shuchinae, China, Asia. Shuchin 4 is a member of a novel family of antimicrobial peptides and has shown antimicrobial activity against various microorganisms, Gram-positive S. aureus, B. cereus, Gram-negative E. coli, B. dysenteriae, P. aeruginosa, and fungus C. albicans (MIC 12-50 ug/ml). Shuchin 4 shows little hemolysis at 200 ug/ml.
The precursor of Shuchin 4 is composed of 64 amino acid residues, including a signal peptide sequence, a spacer peptide fragment, and the mature antimicrobial peptide. The precursor undergoes trypsin-like enzyme processing to release the mature Shuchin 4 peptide. The C-terminus of Shuchin 4 is amidated, and it contains an intramolecular disulfide bridge.

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

• Pei J, Zhao G, Wang B, Wang H. Three novel antimicrobial peptides from the skin of Rana shuchinae. Gene. 2013;521(2):234-7.

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.