ArticleChemical science2026
Distinct adsorption behavior and structures of cell-penetrating peptides at a model lipid membrane interface: a heterodyne-detected vibrational sum frequency generation spectroscopy study.
Article in Chemical science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Arginine-rich cell-penetrating peptides (CPPs) are widely used as molecular delivery vectors, yet the molecular mechanism of their membrane activity and how they penetrate a cell remain unclear. Here, we investigate the interfacial structures of positively charged octa-arginine (R8) and its hydrophobically modified analogue, stearyl-octa-arginine (SR8), at negatively charged lipid monolayers using phase-resolved heterodyne-detected vibrational sum-frequency generation (HD-VSFG) spectroscopy. HD-VSFG measurements show that R8 significantly decreases the intensity of the positive OH stretch band of interfacial water, while SR8 changes it to a negative band. This suggests that the hydrophobic stearyl moiety in SR8 promotes higher adsorption efficiency, inducing charge inversion. In the amide I region, R8 exhibits two spectral components at ∼1640 and ∼1680 cm
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