D(b)PA peptide

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

Batch to batch variation of the purity

• SSLENFRAYV peptide is an important peptide in the field of immunology. It is an H2-Dᵇ restricted influenza peptide derived from the acid polymerase subunit 1 protein (PA224).
• This peptide plays a crucial role in the immune response against influenza virus. It exhibits type II constraints, where the conformation of the peptide is characterized by a pronounced C-terminal arch centered on the critical TCR contact residue, P7-Arg. P7-Arg interacts with the MHC-oriented aromatic rings of P6-Phe and P9-Tyr through its side chain and main chain, respectively. These interactions are significant as they contribute to the overall conformation and antigenicity of the peptide. The peptide is involved in the recognition by cytotoxic T lymphocytes (CTLs), and any alteration in its structure, such as the alanine substitution of P6-Phe (resulting in the variant SSLENARAYV), can lead to a loss of DbPA₂₂₄-specific CTL recognition. This indicates that the peptide's structure and the interactions within it are crucial for its immunological function and its ability to induce an effective immune response against the influenza virus. Overall, SSLENFRAYV peptide is an important molecule for understanding the immune response to influenza and for potential applications in vaccine development and antiviral immunity research.

• Theodossis A, Guillonneau C, Welland A, Ely LK, Clements CS, Williamson NA, Webb AI, Wilce JA, Mulder RJ, Dunstone MA, Doherty PC, McCluskey J, Purcell AW, Turner SJ, Rossjohn J. Constraints within major histocompatibility complex class I restricted peptides: presentation and consequences for T-cell recognition. Proc Natl Acad Sci U S A. 2010 Mar 23;107(12):5534-9. doi: 10.1073/pnas.1000032107. Epub 2010 Mar 8. PMID: 20212169; PMCID: PMC2851776.

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.