corisin peptide

corisin peptide

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

H-IVMPESSGNPNAVNPAGYR-OH

H-Ile-Val-Met-Pro-Glu-Ser-Ser-Gly-Asn-Pro-Asn-Ala-Val-Asn-Pro-Ala-Gly-Tyr-Arg-OH

19

95.65%

C₈₄H₁₃₃N₂₅O₂₈S

1973.16

Synthetic

Powder

Corisin is a pro-apoptotic peptide that is released by Staphylococcus nepalensis, a type of bacteria found in the lungs of patients with idiopathic pulmonary fibrosis (IPF). The sequence of corisin corresponds to a segment of transglycosylase 351 IsaA (MW: 25.6 kDa) of Staphylococcus nepalensis strain CNDG.This peptide induces apoptosis (cell death) of lung epithelial cells, which plays a role in the progression of IPF, suggesting that corisin may be involved in the acute exacerbation of IPF. The discovery of corisin and its role in inducing apoptosis of lung epithelial cells in IPF patients provides insights into the molecular basis for the elevation of staphylococci in pulmonary fibrosis. This finding may lead to the development of new therapeutic strategies for IPF, such as targeting corisin or the bacteria that produce it.

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

• D'Alessandro-Gabazza CN, Kobayashi T, Yasuma T, Toda M, Kim H, Fujimoto H, Hataji O, Takeshita A, Nishihama K, Okano T, Okano Y, Nishii Y, Tomaru A, Fujiwara K, D'Alessandro VF, Abdel-Hamid AM, Ren Y, Pereira GV, Wright CL, Hernandez A, Fields CJ, Yau PM, Wang S, Mizoguchi A, Fukumura M, Ohtsuka J, Nosaka T, Kataoka K, Kondoh Y, Wu J, Kawagishi H, Yano Y, Mackie RI, Cann I, Gabazza EC. A Staphylococcus pro-apoptotic peptide induces acute exacerbation of pulmonary fibrosis. Nat Commun. 2020 Mar 24;11(1):1539. doi: 10.1038/s41467-020-15344-3. PMID: 32210242; PMCID: PMC7093394.

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.