Novel class of peptides disintegrating biological membranes to aid in the characterization of membrane proteins.

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F24%3A00586016" target="_blank" >RIV/61388971:_____/24:00586016 - isvavai.cz</a>
Alternative codes found
RIV/86652036:_____/24:00586016 RIV/67985823:_____/24:00586016 RIV/68378050:_____/24:00586016
Result on the web
<a href="https://www.sciencedirect.com/science/article/pii/S0021925824016491?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0021925824016491?via%3Dihub</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.jbc.2024.107154" target="_blank" >10.1016/j.jbc.2024.107154</a>

Result language
angličtina
Original language name
Novel class of peptides disintegrating biological membranes to aid in the characterization of membrane proteins.
Original language description
Styrene-maleic acid (SMA) and similar amphiphilic copolymers are known to cut biological membranes into lipid nanoparticles/nanodiscs containing membrane proteins apparently in their relatively native membrane lipid environment. Our previous work demonstrated that membrane raft microdomains resist such disintegration by SMA. The use of SMA in studying membrane proteins is limited by its heterogeneity and the inability to prepare defined derivatives. In the present paper, we demonstrate that some amphiphilic peptides structurally mimicking SMA also similarly disintegrate cell membranes. In contrast to the previously used copolymers, the simple peptides are structurally homogeneous. We found that their membrane-disintegrating activity increases with their length (reaching optimum at 24 amino acids) and requires a basic primary structure, that is, (XXD)n, where X represents a hydrophobic amino acid (optimally phenylalanine), D aspartic acid, and n is the number of repeats of these triplets. These peptides may provide opportunities for various well-defined potentially useful modifications in the study of membrane protein biochemistry. Our present results confirm a specific character of membrane raft microdomains.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10608 - Biochemistry and molecular biology

Project
<a href="/en/project/GA19-04047S" target="_blank" >GA19-04047S: Biochemical studies of membrane rafts and immunoreceptors based on cell membrane-disintegrating copolymers</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2024
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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