0586016 - ÚMG 2025 RIV NL eng J - Journal Article
Hořejší, Václav - Angelisová, Pavla - Pokorná, Jana - Charnavets, Tatsiana - Benada, Oldřich - Čajka, Tomáš - Brdička, Tomáš
Novel class of peptides disintegrating biological membranes to aid in the characterization of membrane proteins.
Journal of Biological Chemistry. Roč. 300, č. 4 (2024), č. článku 107154. ISSN 0021-9258. E-ISSN 1083-351X
R&D Projects: GA ČR(CZ) GA19-04047S
Research Infrastructure: CIISB III - 90242
Institutional support: RVO:68378050 ; RVO:67985823 ; RVO:61388971 ; RVO:86652036
Keywords : Styrene-maleic acid * peptides * lipid raft * membrane proteins * lymphocyte * leukocyte
OECD category: Biochemistry and molecular biology; Biochemistry and molecular biology (BTO-N); Analytical chemistry (FGU-C); Biochemistry and molecular biology (MBU-M)
Impact factor: 4, year: 2023 ; AIS: 1.469, rok: 2023
Method of publishing: Open access
Result website:
https://www.sciencedirect.com/science/article/pii/S0021925824016491?via%3DihubDOI: https://doi.org/10.1016/j.jbc.2024.107154

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.
Permanent Link: https://hdl.handle.net/11104/0353629