An Amphiphilic Sulfonatocalix[5]arene as an Activator for Membrane Transport of Lysine-rich Peptides and Proteins
Autor(en): | Pan, Yu-Chen Barba-Bon, Andrea Tian, Han-Wen Ding, Fei Hennig, Andreas Nau, Werner M. Guo, Dong-Sheng |
Stichwörter: | activators; AGGREGATION; ARGININE; calixarenes; CELL-PENETRATING PEPTIDES; Chemistry; Chemistry, Multidisciplinary; DNA; GUANIDINIUM; HYDRATION; INTRACELLULAR DELIVERY; lysine; membrane transport; molecular recognition; MOLECULAR TWEEZERS; SELECTIVE BINDING; TRANSLOCATION | Erscheinungsdatum: | 2021 | Herausgeber: | WILEY-V C H VERLAG GMBH | Enthalten in: | ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | Band: | 60 | Ausgabe: | 4 | Startseite: | 1875 | Seitenende: | 1882 | Zusammenfassung: | Lysine (K) is an important target residue for protein and peptide delivery across membranes. K is the most frequently exposed residue in proteins, leading to high demand for the development of K-compatible transport activators. However, designing activators for K-rich peptides and proteins is more challenging than for arginine-rich species because of the kosmotropic nature of K and its recognition difficulty. In this study, we designed a new amphiphilic sulfonatocalix[5]arene (sCx5-6C) as a K-compatible transport activator. sCx5-6C was tailored with two key elements, recognition of K and the ability to embed into membranes. We measured the membrane transport efficiencies of alpha-poly-l-lysine, heptalysine, and histones across artificial membranes and of alpha-poly-l-lysine into live cells, activated by sCx5-6C. The results demonstrate that sCx5-6C acts as an efficient activator for translocating K-rich peptides and proteins, which cannot be achieved by known arginine-compatible activators. |
ISSN: | 14337851 | DOI: | 10.1002/anie.202011185 |
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