C16G2cys peptide

C16G2cys peptide

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

H-TFFRLFNRSFTQALGKGGGKNLRIIRKGIHIIKKYGGGC-OH

H-Thr-Phe-Phe-Arg-Leu-Phe-Asn-Arg-Ser-Phe-Thr-Gln-Ala-Leu-Gly-Lys-Gly-Gly-Gly-Lys-Asn-Leu-Arg-Ile-Ile-Arg-Lys-Gly-Ile-His-Ile-Ile-Lys-Lys-Tyr-Gly-Gly-Gly-Cys-OH

39

95.2%

C₁₉₉H₃₂₃N₆₁O₄₇S

4354.12

Synthetic

Powder

Streptococcus mutans. Bacterial resistance is becoming a global issue due to its rapid growth. Potential new drugs as antimicrobial peptides (AMPs) are considered for several decades as promising candidates to circumvent this threat. Nonetheless, AMPs have also been used more recently in other settings such as molecular probes grafted on biosensors able to detect whole bacteria. Rapid, reliable and cost-efficient diagnostic tools for bacterial infection could prevent the spread of the pathogen from the earliest stages. Biosensors based on AMPs would enable easy monitoring of potentially infected samples, thanks to their powerful versatility and integrability in pre-existent settings. AMPs, which show a broad spectrum of interactions with bacterial membranes, can be tailored in order to design ubiquitous biosensors easily adaptable to clinical settings. This review aims to focus on the state of the art of AMPs used as the recognition elements of whole bacteria in label-free biosensors with a particular focus on the characteristics obtained in terms of threshold, volume of sample analysable and medium, in order to assess their workability in real-world applications.

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

• Pardoux É, Boturyn D, Roupioz Y. Antimicrobial Peptides as Probes in Biosensors Detecting Whole Bacteria: A Review. Molecules. 2020 Apr 24;25(8):1998.
• Lillehoj, P.B.; Kaplan, C.W.; He, J.; Shi, W.; Ho, C.-M. Rapid, Electrical Impedance Detection of Bacterial Pathogens Using Immobilized Antimicrobial Peptides. J. Lab. Autom. 2013, 19, 42–49.

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.