human Histatin 5 peptide

human Histatin 5 peptide

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

Batch to batch variation of the purity

DSHAKRHHGYKRKFHEKHHSHRGY

Asp-Ser-His-Ala-Lys-Arg-His-His-Gly-Tyr-Lys-Arg-Lys-Phe-His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr

24

98.3%

C₁₃₃H₁₉₅N₅₁O₃₃

3036.2

Synthetic

Powder

Active against C. albicans. Histatin 5 is a proteolytic product of histatin 3. The active domain of histitin 5 (Dh-5) corresponding to residues 11-24 showed HIV inhibitory effects. However,the results with the Dh-5 mutants are mixed (Groot et al. 2006 J. Virol. 80: 9236-9243). The sequence of Dhvar4 is KRLFKKLLFSLRKY, a helical peptide which is active against bacteria and fungi. Dhvar5 has a sequence LLLFLLKKRKKRKY, which is active against bacteria and fungi (Ruissen AL et al 2002 Peptides 23:1391-9). P-113 (P113) is a 12-residue active peptide corresponding to residues 4-15 of histatin 5 (Rothstein DM et al. 2001 AAC 45: 1367). Both the D and L forms (D=L) were equally active against C. albicans, but only the D-form (P113-D) was active in vivo (Sajjan US et al 2001 Antimicrob Agents Chemother 45:3437-3444). The His-His sequence is a good ligand for Cu2+ (Kulon K et al. 2008 J Inorg Biochem 102: 960-72). Enzyme inhibitor: Hst 5 is a competitive cysteine proteinase inhibitor (Gusman H et al., 2001). Derivatives were subjected to clinical trials. human Histatin 5 was found in Homo sapiens.

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

• Oppenheim FG, Xu T, Mcmillian FM, et al. Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans. J Biol Chem. 1988;263(16):7472-7.

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.