AI Article Synopsis
- The study focuses on how changes in cellular membrane shape are crucial for many biological processes, particularly through local curvature changes triggered by specific proteins like Epsin-1.
- Epsin-1's N-terminal segment, EpN18, is identified as key to creating these curvatures, with research revealing important structural features that influence this process.
- Findings highlight that hydrophobic residues, especially leucine, significantly enhance the membrane interaction and curvature induction of EpN18, potentially aiding in the delivery of other molecules into cells.
Article Abstract
Spatiotemporal structural alterations in cellular membranes are the hallmark of many vital processes. In these cellular events, the induction of local changes in membrane curvature often plays a pivotal role. Many amphiphilic peptides are able to modulate membrane curvature, but there is little information on specific structural factors that direct the curvature change. Epsin-1 is a representative protein thought to initiate invagination of the plasma membrane upon clathrin-coated vesicles formation. Its N-terminal helical segment (EpN18) plays a key role in inducing positive membrane curvature. This study aimed to elucidate the essential structural features of EpN18 in order to better understand general curvature-inducing mechanisms, and to design effective tools for rationally controlling membrane curvature. Structural dissection of peptides derived from EpN18 revealed the decisive contribution of hydrophobic residues to (i) enhancing membrane interactions, (ii) helix structuring, (iii) inducing positive membrane curvature, and (iv) loosening lipid packing. The strongest effect was obtained by substitution with leucine residues, as this EpN18 analog showed a marked ability to promote the influx of octa-arginine cell-penetrating peptides into living cells.
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| http://dx.doi.org/10.1002/chem.202300129 | DOI Listing |
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