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http://dx.doi.org/10.1038/s41589-023-01399-y | DOI Listing |
ACS Appl Mater Interfaces
January 2025
Department of Chemistry, Iowa State University, Ames, Iowa 50011-3111, United States.
Intracellular delivery of proteins can directly impact dysregulated and dysfunctional proteins and is a key step in the fast growing field of protein therapeutics. The vast majority of protein-delivery systems enter cells through endocytic pathways, but endosomal escape is a difficult and inefficient process, demanding fundamentally different methods of delivery. We report ultrasmall cationic molecularly imprinted nanoparticles that bind protein targets with high specificity through their uniquely distributed surface lysine groups.
View Article and Find Full Text PDFACS Appl Mater Interfaces
January 2025
Drug Research Program, Division of Pharmaceutical Chemistry and Technology, University of Helsinki, 00014 Helsinki, Finland.
Commun Chem
December 2024
Tagworks Pharmaceuticals, Nijmegen, The Netherlands.
J Control Release
December 2024
School of Nanoscience and Engineering, School of Chemical Sciences, University of Chinese Academy of Sciences, Beijing 101408, China; The Comprehensive Breast Care Center, the Second Affiliated Hospital of Xi'an Jiaotong University, Xi'an 710061, China. Electronic address:
Antithrombotic drugs are widely used to prevent thrombotic events in patients with cardiovascular diseases. However, they all carry varying degrees of bleeding risk. Currently, there are no approved reversal agents for antiplatelet medications, which limits their further clinical application and poses challenges in managing bleeding complications.
View Article and Find Full Text PDFToxins (Basel)
December 2024
Research Department for Limnology, University of Innsbruck, Mondseestrasse 9, 5310 Mondsee, Austria.
Recently, the use of click chemistry for localization of chemically modified cyanopeptides has been introduced, i.e., taking advantage of promiscuous adenylation (A) domains in non-ribosomal peptide synthesis (NRPS), allowing for the incorporation of clickable non-natural amino acids (non-AAs) into their peptide products.
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