PSM α1 (H9BRQ5) peptide

PSM α1 (H9BRQ5) peptide

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

H-MGIIAGIIKVIKSLIEQFTGK-OH

H-Met-Gly-Ile-Ile-Ala-Gly-Ile-Ile-Lys-Val-Ile-Lys-Ser-Leu-Ile-Glu-Gln-Phe-Thr-Gly-Lys-OH

21

95.96%

C₁₀₅H₁₈₃N₂₅O₂₇S

2259.78

Synthetic

Powder

Members of the Staphylococcus aureus phenol-soluble modulin (PSM) peptide family are secreted as functional amyloids that serve diverse roles in pathogenicity and may be present as full-length peptides or as naturally occurring truncations. PSMα1 and PSMα4, involved in biofilm structuring, form canonical cross-β amyloid fibrils wherein β-sheets tightly mate through steric zipper interfaces, conferring high stability. Fibrillation of PSMα1 promotes biofilm stability by preventing disassembly by matrix-degrading enzymes and mechanical stress. PSMα1 and PSMα4 form prototypical amyloid fibrils, while PSMα3 forms cross-α fibrils. PSMα1 and PSMα4 form cross-β fibrils which likely play a role in stabilizing the biofilm matrix.

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

• Salinas N, Colletier JP, Moshe A, Landau M. Extreme amyloid polymorphism in Staphylococcus aureus virulent PSMα peptides. Nat Commun. 2018 Aug 29;9(1):3512.

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.