2018年9月24日
Modular Redesign of a Cationic Lytic Peptide To Promote the Endosomal Escape of Biomacromolecules.
Angewandte Chemie (International ed. in English)
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- 巻
- 57
- 号
- 39
- 開始ページ
- 12771
- 終了ページ
- 12774
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1002/anie.201807534
- 出版者・発行元
- WILEY-V C H VERLAG GMBH
Endocytosis is an important route for the intracellular delivery of biomacromolecules, wherein their inefficient endosomal escape into the cytosol remains a major barrier. Based on the understanding that endosomal membranes are negatively charged, we focused on the potential of cationic lytic peptides for developing endosomolysis agents to release such entrapped molecules. As such, a venom peptide, Mastoparan X, was employed and redesigned to serve as a delivery tool. Appending a tri-glutamate unit to the N-terminus attenuates the cytotoxicity of Mastoparan X by about 40 fold, while introduction of a NiII -dipicolylamine complex enhances cellular uptake of the peptide by about 17 fold. Using the optimized peptide, various fluorescently labeled macromolecules were successfully delivered to the cytosol, enabling live-cell imaging of acetylated histones.
- リンク情報
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- DOI
- https://doi.org/10.1002/anie.201807534
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/30101453
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000444941600027&DestApp=WOS_CPL
- Scopus
- https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85053278356&origin=inward
- Scopus Citedby
- https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=85053278356&origin=inward
- ID情報
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- DOI : 10.1002/anie.201807534
- ISSN : 1433-7851
- eISSN : 1521-3773
- PubMed ID : 30101453
- SCOPUS ID : 85053278356
- Web of Science ID : WOS:000444941600027