| Product Name | N-peptide |
|---|---|
| Description | 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. |
| Synonyms | antibiotic resistance, bacteria, gram-negative, AM-185, AM185, N-peptide, OMP, PPIase, WEYIPNV, outer membrane porins, peptidyl-prolyl isomerase, periplasmic chaperone protein chaperone SurA |
| Molecular Weight | 920.03 Da |
| Target | Protein-protein interactions |
| Amino Acid Sequence | WEYIPNV |
| Form | Freeze dried solid |
| Purity | >95% by HPLC |
| Storage | We recommend storage desiccated, frozen and in the dark |
| Notes | Modifications: None |
| References |
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: 14506253Xu 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: 17825319Bell 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 areasAll peptides >All protein-protein interaction modulators >All antibacterials > |
| Supplier | Isca Biochemicals Limited |
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