UBI (31-38) 

UBI (31-38) is a Ubiquicidin-derived octapeptide and anti-bacterial agent. UBI (31-38) selectively interacts with anionic phospholipid membranes and restricts lipid lateral motion. UBI (31-38) induces anionic vesicle aggregation via electrostatic repulsion screening, and undergoes conformational changes in membrane-mimicking environments. UBI (31-38) can be used for the research of infection imaging probes^[1].

UBI (31-38) undergoes a random coil-to-structural transition in TFE-containing buffer and in an anionic model bacterial membrane^[1].
UBI (31-38) selectively binds to anionic model bacterial membranes (POPG LUVs) with an association constant of 2.58 × 10⁵/M, while showing no significant interaction with zwitterionic model mammalian membranes (POPC LUVs)^[1].
UBI (31-38) (2 h) uptake by Staphylococcus aureus ATCC 25923 is driven by electrostatic interactions^[1].
UBI (31-38) induces aggregation of anionic model bacterial membranes (POPG LUVs) at peptide-to-lipid molar ratios of 10% and above, with significant aggregation occurring at 40% P/L, while having no effect on zwitterionic model mammalian membranes (POPC LUVs)^[1].
UBI (31-38) (P/L = 4%) restricts the lateral motion of lipids in anionic model bacterial membranes (DPPG LUVs) at a peptide-to-lipid molar ratio of 4%, reducing the lateral diffusion coefficient by 28%, while leaving lipid internal motions unaffected^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

1108.32

C₄₆H₈₁N₁₉O₁₁S

290360-66-6

Arg-Ala-Lys-Arg-Arg-Met-Gln-Tyr

RAKRRMQY

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• [1]. Bhatt Mitra J, et al. Ubiquicidin-Derived Peptides Selectively Interact with the Anionic Phospholipid Membrane. Langmuir. 2020;36(1):397-408.  [Content Brief]