N-peptide

N-peptide

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

Batch to batch variation of the purity

H-WEYIPNV-OH

H-Trp-Glu-Tyr-Ile-Pro-Asn-Val-OH

7

95.71%

C₄₅H₆₁N₉O₁₂

920.01

Synthetic

Powder

N-peptide, WEYIPNV, is a heptapeptide selected from a phage library that binds the gram-negative, periplasmic chaperone protein chaperone SurA with micromolar affinity. N-peptide (WEYIPNV) recognition is conferred by the first peptidyl-prolyl isomerase (PPIase) domain of SurA and N-peptide and SurA bind to each other in a 1:1 ratio. SurA is involved in the proper folding of outer membrane porins (OMPs), which protect bacteria against toxins in the extracellular environment and novel SurA inhibitors have the potential to overcome antibiotic resistance. Rhodamine-labeled N-peptide WEYIPNV can be used for a competitive assay for inhibitors of SurA.

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

• Bitto and McKay (2003) The Periplasmic Molecular Chaperone Protein SurA Binds a Peptide Motif That Is Characteristic of Integral Outer Membrane Proteins. J.Biol.Chem. 278 49316 PMID: 14506253
• Xu et al (2007) The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues. J. Mol. Biol. 373(2) 367 PMID: 17825319
• Bell et al (2018) Identification of inhibitors of the E. coli chaperone SurA using in silico and in vitro techniques. Bioorg. Med. Chem. Lett. 28(22) 3540 PMID: 30301675

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.