Journal Article PUBDB-2017-13499

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Lipid-like Peptides can Stabilize Integral Membrane Proteins for Biophysical and Structural Studies

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2017
Wiley-VCH Weinheim

ChemBioChem 18(17), 1735 - 1742 () [10.1002/cbic.201700235]
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Abstract: A crucial bottleneck in membrane protein structural biology is the difficulty in identifying a detergent that can maintain the stability and functionality of integral membrane proteins (IMPs). Detergents are poor membrane mimics, and their common use in membrane protein crystallography may be one reason for the challenges in obtaining high-resolution crystal structures of many IMP families. Lipid-like peptides (LLPs) have detergent-like properties and have been proposed as alternatives for the solubilization of G protein-coupled receptors and other membrane proteins. Here, we systematically analyzed the stabilizing effect of LLPs on integral membrane proteins of different families. We found that LLPs could significantly stabilize detergent-solubilized IMPs in vitro. This stabilizing effect depended on the chemical nature of the LLP and the intrinsic stability of a particular IMP in the detergent. Our results suggest that screening a subset of LLPs is sufficient to stabilize a particular IMP, which can have a substantial impact on the crystallization and quality of the crystal.

Classification:

Note: (c) The Authors PIF‐2014‐33

Contributing Institute(s):
  1. CSSB-EMBL (CSSB-EMBL)
  2. CSSB-EMBL-CL (CSSB-EMBL-CL)
Research Program(s):
  1. 6G3 - PETRA III (POF3-622) (POF3-622)
Experiment(s):
  1. PETRA Beamline P13 (PETRA III)

Appears in the scientific report 2017
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Medline ; Creative Commons Attribution CC BY 4.0 ; OpenAccess ; BIOSIS Previews ; Current Contents - Life Sciences ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection
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 Record created 2017-12-14, last modified 2025-07-30


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