BMAP-27 peptide

BMAP-27 peptide

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

Batch to batch variation of the purity

H-GRFKRFRKKFKKLFKKLSPVIPLLHL-NH2

H-Gly-Arg-Phe-Lys-Arg-Phe-Arg-Lys-Lys-Phe-Lys-Lys-Leu-Phe-Lys-Lys-Leu-Ser-Pro-Val-Ile-Pro-Leu-Leu-His-Leu-NH2

26

95.2%

C₁₅₈H₂₆₃N₄₅O₂₇

3225.05

Synthetic

Powder

BMAP-27 is a membranolytic helical peptide. Upon interaction with bacterial membranes, BMAP-27 acquires an amphipathic α-helical conformation, with the polar sector of the cylinder characterized by the presence of numerous positively charged residues, and the opposite one having a markedly hydrophobic character. This configuration favours interaction with, and insertion into, the bacterial membrane, and the peptides then aggregate to form pores and/or disaggregates the membranes by the so-called “carpet mechanism” in a concentration dependent manner. BMAP-27 is induced to adopt a α-helical conformation in the presence of EPOLs from BF produced by all three strains, KpTs101, KpTs113, and KpMn7, but to different extents.

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

• Bellich B, Lagatolla C, Tossi A, Benincasa M, Cescutti P, Rizzo R. Influence of Bacterial Biofilm Polysaccharide Structure on Interactions with Antimicrobial Peptides: A Study on Klebsiella pneumoniae. Int J Mol Sci. 2018;19(6)

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.