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N-peptide
Cat. No. AM-185
Structure:
H-Trp-Glu-Tyr-Ile-Pro-Asn-Val-OH
Activity:
Binds the periplasmic chaperone protein chaperone SurA
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.
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
Related areas
All peptides >
All protein-protein interaction modulators >
All antibacterials >
Technical Data
| Structure | H-Trp-Glu-Tyr-Ile-Pro-Asn-Val-OH |
| Molecular Weight | 920.03 |
| Formula | C45H61N9O12 |
| Sequence | WEYIPNV |
| Modifications | None |
Solubility and Storage
| Solubility | Soluble in water |
| Appearance | Freeze dried solid |
| Storage | We recommend storage desiccated, frozen and in the dark |
Batch Specific Data
| Purity | >95% by HPLC |
| Safety Data Sheet | N-peptide MSDS_602c01aebd12b.pdf |
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Recent citations
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