KW- peptide

KW- peptide

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

H-EEFKWKFKEE-OH

H-Glu-Glu-Phe-Lys-Trp-Lys-Phe-Lys-Glu-Glu-OH

10

95.12%

C₆₇H₉₄N₁₄O₁₉

1399.54

Synthetic

Powder

A robust two-component hydrogel from complementary decapeptides, KW+/p2 (KKFEWEFEKK) and KW-/p1 (EEFKWKFKEE). The design of these complementary peptides included the simple ‘hphphp’ repeating pattern (h = hydrophobic residue, p = polar residue) that is known to favour β-sheet structures, with tryptophan included to enhance aromatic pairing interactions and to allow peptide concentrations to be accurately determined. Hydrogels are produced by the self-assembly of peptides p1 + p2 into antiparallel β-sheets, which undergo hierarchical self-assembly into different fibrillar structures including large twisted fibres.

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

• King PJ, Giovanna Lizio M, Booth A, Collins RF, Gough JE, Miller AF, Webb SJ. A modular self-assembly approach to functionalised β-sheet peptide hydrogel biomaterials. Soft Matter. 2016 Feb 14;12(6):1915-23. doi: 10.1039/c5sm02039e. Epub 2016 Jan 6. PMID: 26702608.

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.