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Products
Pharmacology
Type
- News
- Custom services
- Ordering
- About Us
- Technical support
- Resources
BING
Cat. No. AM-280
Structure:
Other Names:
Activity:
BING is an antimicrobial peptide found in the plasma of the Japanese rice fish medaka (Oryzias latipes), derived from vacuolar protein sorting-associated protein 13D-like (Vps13D). BING possesses toxicity against a broad range of gram-positive and negative bacteria including drug resistant strains, at concentrations that have low toxicity to mammalian cell lines. BING treatment induces deregulation of periplasmic peptidyl-prolyl isomerases in gram-negative bacteria and also reduces the RNA level of cpxR, an upstream regulator of envelope stress responses which plays a crucial role in the development of antimicrobial resistance.
Dong et al (2021) BING, a novel antimicrobial peptide isolated from Japanese medaka plasma, targets bacterial envelope stress response by suppressing cpxR expression. Sci Rep. 11(1) 12219 PMID: 34108601
Related areas
Technical Data
| Structure | H-Ile-Arg-Ile-Ile-Leu-Arg-Ala-Gln-Gly-Ala-Leu-Lys-Ile-OH |
| Molecular Weight | 1464.86 |
| Formula | C67H125N21O15 |
| Sequence | IRIILRAQGALKI |
| Modifications | None |
Solubility and Storage
| Solubility | Soluble in water |
| Appearance | Freeze dried solid |
| Storage | Store dry, frozen and in the dark |
Batch Specific Data
| Purity | >95% by hplc |
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Recent citations
A new publication from the University of Ljubljana uses MCA-AVLQSGFR-Lys(Dnp)-Lys-NH2, the FRET substrate for the severe acute respiratory syndrome coronavirus main protease (SARS-CoV Mpro), to determine the inhibitory potential of plant polyphenols
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