Brevinin-1Ma peptide

Brevinin-1Ma peptide

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

Batch to batch variation of the purity

H-FLPILAGLAANLVPKLICSITKKC-NH2

H-Phe-Leu-Pro-Ile-Leu-Ala-Gly-Leu-Ala-Ala-Asn-Leu-Val-Pro-Lys-Leu-Ile-Cys-Ser-Ile-Thr-Lys-Lys-Cys-NH2

24

95.2%

C₁₁₈H₂₀₃N₂₉O₂₇S₂

2524.17

Synthetic

Powder

Brevinin-1Ma is a novel skin defense peptide from the endangered Sierra Nevada yellow-legged frog, R. sierrae. The expression of the peptide was significantly affected by treatment with probiotics, such that addition of a consortium of four anti-Bd bacteria led to the apparent relative reduction of the peptide. The composition of the peptide profile, but not the quantity of total peptides, was altered by the therapy.Brevinin-1Ma was tested against a range of amphibian skin cultures and found to inhibit growth of fungal pathogens Bd and B. salamandrivorans, but enhanced the growth of probiotic bacteria including Janthinobacterium lividum, Chryseobacterium ureilyticum, Serratia grimesii, and Pseudomonas sp. While commonly thought of as antimicrobial peptides, here brevinin-1Ma showed promicrobial function, facilitating microbial growth. Thus, skin exposure to probiotic bacterial cultures induced a shift in skin defense peptide profiles that appeared to act as an immune response functioning to regulate the microbiome. In addition to direct microbial antagonism, probiotic-host interactions may be a critical mechanism affecting disease resistance.

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

• Woodhams DC, Rollins-Smith LA, Reinert LK, et al. Probiotics Modulate a Novel Amphibian Skin Defense Peptide That Is Antifungal and Facilitates Growth of Antifungal Bacteria. Microb Ecol. 2020;79(1):192-202

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.