In:
eLife, eLife Sciences Publications, Ltd, Vol. 7 ( 2018-08-15)
Abstract:
Surrounding every living cell is a biological membrane that is largely impermeable to water-soluble molecules. This hydrophobic (or “water-hating”) barrier preserves the contents of the cell and also regulates how the cell interacts with its environment. This latter function is critical and relies on a class of proteins that are embedded within the membrane and are also hydrophobic. The hydrophobic nature of membrane proteins is however inconvenient for biochemical studies which usually take place in water-based solutions. Therefore, membrane proteins are under-represented in biological research compared to the water-soluble ones, even though roughly one quarter of a cell’s proteins are membrane proteins. Researchers have developed a few tricks to keep membrane proteins soluble after they have been extracted from the membrane. An old but popular technique makes use of detergents, which are chemicals with opposing hydrophobic and hydrophilic properties (hydrophilic literally means “water-loving”). However, even mild detergents can damage membrane proteins and will sometimes lead to experimental artifacts. More recent tricks to stabilize membrane proteins without detergents have been described but remain laborious, costly or difficult to perform. To overcome these limitations, Carlson et al. developed a simple method to stabilize membrane proteins without detergent. Called the “peptidisc”, the method uses multiple copies of a unique peptide – a short sequence of the building blocks of protein – that had been redesigned to have optimal hydrophobic and hydrophilic properties. The idea was that the peptides would wrap around the hydrophobic parts of the membrane protein, and shield them from the watery solution. Indeed, when Carlson et al. mixed this peptide with five different membrane proteins from bacteria, all were perfectly soluble and functional without detergent. The ideal ratio of peptide needed to form a peptidisc around each membrane protein was reached automatically, without having to test many different conditions. This indicates that the peptidisc acts like a “one size fits all” scaffold. The peptidisc is a new tool that will allow more researchers, including those who are not expert biochemists, to study membrane proteins. This will yield a better understanding of the structure of a cell’s membrane and how it interacts with the environment. Since the approach is both simple and easy to apply, more membrane proteins can now also be included in high-throughput searches for potential new drugs for various medical conditions.
Type of Medium:
Online Resource
ISSN:
2050-084X
DOI:
10.7554/eLife.34085.001
DOI:
10.7554/eLife.34085.002
DOI:
10.7554/eLife.34085.003
DOI:
10.7554/eLife.34085.004
DOI:
10.7554/eLife.34085.005
DOI:
10.7554/eLife.34085.006
DOI:
10.7554/eLife.34085.007
DOI:
10.7554/eLife.34085.008
DOI:
10.7554/eLife.34085.009
DOI:
10.7554/eLife.34085.010
DOI:
10.7554/eLife.34085.011
DOI:
10.7554/eLife.34085.012
DOI:
10.7554/eLife.34085.013
DOI:
10.7554/eLife.34085.014
DOI:
10.7554/eLife.34085.015
DOI:
10.7554/eLife.34085.016
DOI:
10.7554/eLife.34085.017
DOI:
10.7554/eLife.34085.018
DOI:
10.7554/eLife.34085.019
DOI:
10.7554/eLife.34085.020
DOI:
10.7554/eLife.34085.022
DOI:
10.7554/eLife.34085.023
Language:
English
Publisher:
eLife Sciences Publications, Ltd
Publication Date:
2018
detail.hit.zdb_id:
2687154-3
Permalink