Front Cover: Incubation of Amyloidogenic Peptides in Reverse Micelles Allow Active Control of Oligomer Size and Study of Protein–Protein Interactions (ChemMedChem 23/2024)
Han-Wen Chang, Chien-I Yang, Jerry Chun Chung Chan
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引用次数: 0
Abstract
This cover illustrates the encapsulation of amyloid beta (Aβ) peptides within reverse micelles, symbolizing the controlled aggregation of Aβ oligomers within these nano-sized environments. The reverse micelles facilitate a rapid coalesce-and-separate process, where the Aβ peptides inside are brought together to form oligomers. The size of these oligomers is constrained by the physical dimensions of the reverse micelle, offering a unique way to study their aggregation process in a controlled setting. This artwork captures the dynamic interaction and precise regulation of oligomer size within the micelles. More details can be found in article 10.1002/cmdc.202400310 by Jerry Chun Chung Chan and co-workers.
期刊介绍：
Quality research. Outstanding publications. With an impact factor of 3.124 (2019), ChemMedChem is a top journal for research at the interface of chemistry, biology and medicine. It is published on behalf of Chemistry Europe, an association of 16 European chemical societies.
ChemMedChem publishes primary as well as critical secondary and tertiary information from authors across and for the world. Its mission is to integrate the wide and flourishing field of medicinal and pharmaceutical sciences, ranging from drug design and discovery to drug development and delivery, from molecular modeling to combinatorial chemistry, from target validation to lead generation and ADMET studies. ChemMedChem typically covers topics on small molecules, therapeutic macromolecules, peptides, peptidomimetics, and aptamers, protein-drug conjugates, nucleic acid therapies, and beginning 2017, nanomedicine, particularly 1) targeted nanodelivery, 2) theranostic nanoparticles, and 3) nanodrugs.
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