Membrane Protein Services

Dedicated to membrane protein research, empowering drug discovery

Membrane proteins—including G protein-coupled receptors (GPCRs), ion channels, and transporters—represent one of the most important classes of drug targets, playing pivotal roles in cell signaling, substance transport, and the pathogenesis and progression of diseases.

However, as membrane proteins naturally reside within a lipid bilayer environment—characterized by difficulties in expression, poor stability, complex purification, and challenging structural elucidation—researching them has long posed a significant challenge in the fields of structural biology and drug discovery.

TECHNOLOGY PLATFORM

Distolife has established an integrated technology platform tailored to the needs of membrane protein drug R&D. Covering membrane protein expression, purification, stability optimization, reconstitution in native-like environments, functional validation, and structural analysis support, the platform delivers professional, efficient, and reliable membrane protein solutions to research institutions, biopharmaceutical companies, and drug development teams.

Membrane Protein Technology Workflow

Full-Spectrum Membrane Protein Target Capabilities

Service Highlights

Facilities Introduction

The platform is equipped with multiple world-class instruments, covering key technological stages across the entire membrane protein CRO workflow, thereby ensuring the accuracy of experimental data and the stability and reprehensibility of production processes. 

Case Study

Case 1: Cryo-EM Structure of A2AR-Gs Complex

Introduction:

Distolife membrane protein R&D team purified the target membrane protein—the A_2AR−Gscomplex—using a detergent and phospholipid system. Through cryo-EM structural determination, they solved the 3D protein structure at a resolution of 2.86 Å. This structure shows high consistency with previously published literature while achieving superior resolution.

Case 2: Cryo-EM Structure of GCGR-Gs Complex

Introduction:

Distolife membrane protein R&D team purified the target membrane protein—the GCGR-Gs complex—using the LMNG and CHS system. Through cryo-EM structural determination, they resolved the 3D protein structure at a resolution of 3.69 Å. This structure shows high consistency with previously published literature while achieving superior resolution with a smaller dataset.

Case 3: Cryo-EM Structural Analysis of GCGR-Gs and GCGR-Gi1 Complexes

Introduction：

The Chief Scientific Officer of the Distolife team used cryo-EM to resolve, for the first time, the complex structures of a Class B GPCR—the human glucagon receptor (GCGR)—bound to Gs and Gi1, respectively (3.7/3.9 Å). Combined with NanoBiT, mutation, and signaling assays, the study revealed that the receptor accommodates both G proteins using a common open pocket: Gs achieves biased coupling through a larger interface (802 vs 551 Ų), whereas differences in intracellular loops ICL1/ICL2 dictate selectivity. This revises the traditional model that "pocket size determines specificity," laying a structural foundation for biased drug design.

Case 4: Cryo-EM Structural Analysis of mGlu2–Gi1 and mGlu4–Gi3 Complexes

Introduction ：

The Chief Scientific Officer of the Distolife team used cryo-EM to resolve, for the first time, the fully active complex structures of Class C GPCRs—human mGlu2 and mGlu4 bound to Gi proteins (3.1−4.0Å. Combined with mutagenesis, NanoBiT, and cysteine cross-linking assays, the study revealed that TM6 does not shift outward upon mGlu activation, and the α5C-terminus of Gαibinds to a shallow groove formed by three intracellular loops together with helix III/IV. Furthermore, it demonstrated at atomic resolution for the first time that the asymmetric dimer interface serves as the structural basis for "only one receptor subunit coupling to a G protein," deepening the understanding of GPCR activation.

Case 5: Crystal Structure Determination of Y1R in Complex with Selective Antagonists

Introduction ：

The Chief Scientific Officer of the Distolife team determined the first crystal structures of the neuropeptide Y receptor family—human Y1R in complex with two selective antagonists (2.7/3.0 Å.). Combined with mutagenesis, solid-state NMR, Rosetta docking, and photo-crosslinking, the study elucidated the antagonist binding modes and key selectivity determinants, such as the D287^6.59salt bridge. Furthermore, it identified for the first time the interactions between the N-terminus of the endogenous agonist NPY and the receptor's N-terminus as well as ECL2, laying a structural foundation for designing NPY-targeted drugs against obesity and other diseases.  

Why Distolife vs. Generalist CROs

A specialist membrane-protein CRO, not a one-size-fits-all outsourcing vendor.

Same target. Different outcomes.
— Distolife delivers membrane-protein data that directly drive structure-based drug design.