New structural insights into drug resistance with Salipro®
A recent study published in The EMBO Journal has shed light on how Salipro®-embedded ABCB1 recognizes and transports a wide range of substrates.
Why is this important? ABCB1, also known as P-glycoprotein, is central to drug resistance in cancer and other diseases. Understanding how it recognizes and transports a wide range of substrates is vital for developing more effective therapies.
Role of Salipro® technology: Our Salipro® technology was pivotal in stabilizing ABCB1 in native lipid environments for native-mass spectrometry (nMS), ATPase activity assays and cryoEM.
Superior activity and stability: The Salipro®-ABCB1 particles demonstrated greater ATPase activity and a more homogenous mass distribution - compared to traditional nanodisc reconstitution methods.
High-resolution structural insights: The 3D structures of lipid-embedded human Salipro®-ABCB1 revealed the dynamic structural changes and binding site plasticity that ABCB1 undergoes when interacting with various substrates and inhibitors.
This structural and functional work unlocked with Salipro® deepens our understanding of ABCB1's mechanisms and opens new avenues for developing new drugs to bypass multidrug resistance.
Congratulations to Amer Alan and the entire research team for this contribution to understanding drug interactions and resistance mechanisms!
Read the full study here:
D. Kurre, et al., Structural insights into binding-site access and ligand recognition by human ABCB1. EMBO J. (2025).