Academic Journal

Characterization of membrane protein interactions by peptidisc-mediated mass photometry

التفاصيل البيبلوغرافية
العنوان: Characterization of membrane protein interactions by peptidisc-mediated mass photometry
المؤلفون: John William Young, Emanuel Pfitzner, Raman van Wee, Carla Kirschbaum, Philipp Kukura, Carol V. Robinson
المصدر: iScience, Vol 27, Iss 2, Pp 108785- (2024)
بيانات النشر: Elsevier, 2024.
سنة النشر: 2024
المجموعة: LCC:Science
مصطلحات موضوعية: Biochemistry methods, Biotechnology, Membranes, Science
الوصف: Summary: Membrane proteins perform numerous critical functions in the cell, making many of them primary drug targets. However, their preference for a lipid environment makes them challenging to study using established solution-based methods. Here, we show that peptidiscs, a recently developed membrane mimetic, provide an ideal platform to study membrane proteins and their interactions with mass photometry (MP) in detergent-free conditions. The mass resolution for membrane protein complexes is similar to that achievable with soluble proteins owing to the low carrier heterogeneity. Using the ABC transporter BtuCD, we show that MP can quantify interactions between peptidisc-reconstituted membrane protein receptors and their soluble protein binding partners. Using the BAM complex, we further show that MP reveals interactions between a membrane protein receptor and a bactericidal antibody. Our results highlight the utility of peptidiscs for membrane protein characterization in detergent-free solution and provide a rapid and powerful platform for quantifying membrane protein interactions.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2589-0042
Relation: http://www.sciencedirect.com/science/article/pii/S2589004224000063; https://doaj.org/toc/2589-0042
DOI: 10.1016/j.isci.2024.108785
URL الوصول: https://doaj.org/article/df4467bb30344d189781786f5400db98
رقم الانضمام: edsdoj.f4467bb30344d189781786f5400db98
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:25890042
DOI:10.1016/j.isci.2024.108785