RNase 7 (1-45aa) peptide

RNase 7 (1-45aa) peptide

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

H-RPRGMTSSQWFRIQHMQPSPQASNSAMRNINRHTRRSRDLNTFLH-OH

H-Arg-Pro-Arg-Gly-Met-Thr-Ser-Ser-Gln-Trp-Phe-Arg-Ile-Gln-His-Met-Gln-Pro-Ser-Pro-Gln-Ala-Ser-Asn-Ser-Ala-Met-Arg-Asn-Ile-Asn-Arg-His-Thr-Arg-Arg-Ser-Arg-Asp-Leu-Asn-Thr-Phe-Leu-His-OH

45

95.2%

C₂₂₇H₃₆₄N₈₄O₆₅S₃

5406.01

Synthetic

Powder

Candida albicans is a polymorphic fungus responsible formucosal and skin infections. Candida cells establish themselves into biofilm communities resistant to most currently available antifungal agents. An increase of severe infections ensuing in fungal septic shock in elderly or immunosuppressed patients, along with the emergence of drug-resistant strains, urge the need for the development of alternative antifungal agents. In the search for novel antifungal drugs our laboratory demonstrated that two human ribonucleases from the vertebrate-specific RNaseA superfamily, hRNase3 and hRNase7, display a high anticandidal activity. In a previous work, we proved that the N-terminal region of the RNaseswas sufficient to reproducemost of the parental protein bactericidal activity. Next, we explored their potency against a fungal pathogen. Here, we have tested the N-terminal derived peptides that correspond to the eight human canonical RNases (RN1-8) against planktonic cells and biofilms of C. albicans. RN3 and RN7 peptides displayed the most potent inhibitory effect with a mechanism of action characterized by cell-wall binding,membrane permeabilization and biofilmeradication activities. Both peptides are able to eradicate planktonic and sessile cells, and to alter their gene expression, reinforcing its role as a lead candidate to develop novel antifungal and antibiofilm therapies.

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

• Salazar VA, Arranz-Trullu00e9n J, Prats-Ejarque G, et al. Insight into the Antifungal Mechanism of Action of Human RNase N-terminus Derived Peptides. Int J Mol Sci. 2019;20(18):4558. Published 2019 Sep 14. doi:10.3390/ijms20184558

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.