Hydrophobicity is a key determinant in the activity of arginine-rich cell penetrating peptides

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 2045-2322

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: Hydrophobicity is a key determinant in the activity of arginine-rich cell penetrating peptides ; volume:12 ; number:1 ; day:25 ; month:9 ; year:2022 ; pages:1-12 ; date:12.2022
Scientific reports ; 12, Heft 1 (25.9.2022), 1-12, 12.2022

Creator: Allen, Jason
Pellois, Jean-Philippe

Contributor: SpringerLink (Online service)

DOI: 10.1038/s41598-022-20425-y

URN: urn:nbn:de:101:1-2022121221144226070417

Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 15.08.2025, 7:24 AM CEST

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Allen, Jason
Pellois, Jean-Philippe
SpringerLink (Online service)

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Hydrophobicity is a key determinant in the activity of arginine-rich cell penetrating peptides

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Other Objects (12)

Hydrophobicity of arginine leads to reentrant liquid-liquid phase separation behaviors of arginine-rich proteins

Prediction of Cell-Penetrating Peptides

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Prediction of twin-arginine signal peptides

Internalization mechanisms of cell-penetrating peptides

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Hydrophobicity of arginine leads to reentrant liquid-liquid phase separation behaviors of arginine-rich proteins

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Prediction of twin-arginine signal peptides

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Hydrophobicity of arginine leads to reentrant liquid-liquid phase separation behaviors of arginine-rich proteins

Prediction of Cell-Penetrating Peptides

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Prediction of twin-arginine signal peptides

Internalization mechanisms of cell-penetrating peptides

Arginine and Tryptophan rich antimicrobial peptides (AMP)

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