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TitleDeFrND: detergent-free reconstitution into native nanodiscs with designer membrane scaffold peptides.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 7973, Year 2025
Publish dateAug 26, 2025
AuthorsQian Ren / Jing Wang / Vinay Idikuda / Shanwen Zhang / Jeehae Shin / W Grant Ludlam / Luis M Real Hernandez / Sara Zdancewicz / Alex J B Kreutzberger / Hucheng Chang / Volker Kiessling / Lukas K Tamm / Ahmad Jomaa / Ilya Levental / Kirill Martemyanov / Baron Chanda / Huan Bao /
PubMed AbstractMembrane scaffold protein-based nanodiscs have facilitated unprecedented structural and biophysical analysis of membrane proteins in a near-native lipid environment. However, successful ...Membrane scaffold protein-based nanodiscs have facilitated unprecedented structural and biophysical analysis of membrane proteins in a near-native lipid environment. However, successful reconstitution of membrane proteins in nanodiscs requires prior solubilization and purification in detergents, which may impact their physiological structure and function. Furthermore, the detergent-mediated reconstitution of nanodiscs is unlikely to recapitulate the precise composition or asymmetry of native membranes. To circumvent this fundamental limitation of traditional nanodisc technology, we herein describe the development of membrane-solubilizing peptides to directly extract membrane proteins from native cell membranes into nanoscale discoids. By systematically protein engineering and screening, we create a class of chemically modified Apolipoprotein-A1 mimetic peptides to enable the formation of detergent-free nanodiscs with high efficiency. Nanodiscs generated with these engineered membrane scaffold peptides are suitable for obtaining high-resolution structures using single-particle cryo-EM with native lipids. To further highlight the versatility of our approach, we directly extract a sampling of membrane signaling proteins with their surrounding native membranes for biochemical and biophysical interrogations.
External linksNat Commun / PubMed:40858559 / PubMed Central
MethodsEM (single particle)
Resolution3.26 - 3.51 Å
Structure data

44435

9bcr

EMDB-44435, PDB-9bcr:
Cryo-EM structure of a bacterial prototype ATP-binding cassette transporter MalFGK2.
Method: EM (single particle) / Resolution: 3.26 Å

49659

9nqj

EMDB-49659, PDB-9nqj:
Cryo-EM structure of a bacterial prototype ATP-binding cassette transporter MalFGK2.
Method: EM (single particle) / Resolution: 3.34 Å

49901

9nxc

EMDB-49901, PDB-9nxc:
Cryo-EM structure of a bacterial prototype ATP-binding cassette transporter MalFGK2.
Method: EM (single particle) / Resolution: 3.51 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-VO4:
VANADATE ION

Source
  • escherichia coli k-12 (bacteria)
  • escherichia coli (E. coli)
KeywordsTRANSPORT PROTEIN / bacterial prototype ATP-binding cassette transporter

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