BMAP-28 (BMAP28) peptide

BMAP-28 (BMAP28) peptide

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

GGLRSLGRKILRAWKKYGPIIVPIIRIG

H-Gly-Gly-Leu-Arg-Ser-Leu-Gly-Arg-Lys-Ile-Leu-Arg-Ala-Trp-Lys-Lys-Tyr-Gly-Pro-Ile-Ile-Val-Pro-Ile-Ile-Arg-Ile-Gly-OH

28

96%

C₁₄₇H₂₅₂N₄₄O₃₁

3131.8

Synthetic

Powder

Active against E. coli, S. typhimurium, P. aeruginosa, S. marcescens, S. aureus (MRSA), S. epidermidis, B. megaterium (MIC 0.5-4 uM), C. albicans, and C. neoformans (MIC 4-8 uM). BMAP-28 has broad antimicrobial activities and confers protection in an animal model:mouse of bacterial infection or sepsis (Giacometti A et al. 2004 Crit Care Med 32, 2485-90). Furthermore, BMAP-28 and its isomers demonstrated anti-leishmanial activities against intracellular L. major amastigotes within a macrophage infection model. Interestingly, the D-amino acid form is more active against parasites than either BMAP-28 (the L form) or the sequence reversed form (Lynn MA et al 2011 PLoS Negl Trop Dis. 5(5):e1141). Trucation of the C-terminal tail reduced hemolysis. Of note, a modified peptide (mBMAP-28) was also synthesized by replacing the C-terminal hydrophobic tail (residues 20-28) with a more hydrophilic sequence QATPATRQ also reduced peptide cell selectivity. Updated 7/2011. BMAP-28 (BMAP28) has Antibacterial, Antifungal activity. The source of BMAP-28 (BMAP28) is Cow Bos taurus.

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

• Skerlavaj B, Gennaro R, Bagella L, Merluzzi L, Risso A, Zanetti M. Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities. J Biol Chem. 1996;271(45):28375-81.

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.