A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Self-Adaptive Synthesis of Non-Covalent Crosslinkers while Folding Single-Chain Polymers
Tekijät: Qi, Dawei; Shi, Xuncheng; Lin, Caihong; Holzhausen, Ferdinand; Ville, Liljeström; Sun, Xun; Luo, Jinghui; Pitkänen, Leena; Zhu, Ya; Rosenholm, Jessica; Jalkanen, Sirpa; Li, Jianwei
Kustantaja: Wiley-VCH
Julkaisuvuosi: 2024
Journal: Angewandte Chemie International Edition
Tietokannassa oleva lehden nimi: Angewandte Chemie (International ed. in English)
Lehden akronyymi: Angew Chem Int Ed Engl
Artikkelin numero: e202408670
Vuosikerta: 63
Numero: 38
ISSN: 1433-7851
eISSN: 1521-3773
DOI: https://doi.org/10.1002/anie.202408670
Verkko-osoite: https://doi.org/10.1002/anie.202408670
Rinnakkaistallenteen osoite: https://research.utu.fi/converis/portal/detail/Publication/457065818
Peptide folding is a dynamic process driven by non-covalent cross-linking leading to functional nanostructures for essential biochemical activities. However, replicating this process in synthetic systems is challenging due to the difficulty in mimicking nature's real-time regulation of non-covalent crosslinking for single-chain polymer folding. Here, we address this by employing anionic dithiol building blocks to create macrocyclic disulfides as non-covalent crosslinkers that adapted to the folding process. Initially, small macrocycles facilitated a low degree folding of a polycation. Then, this preorganized structure catalysed the production of larger macrocycles that enhanced the folding conversely. The self-adaptive synthesis was verified through the encapsulation of an anticancer drug, showing an updated production distribution of non-covalent crosslinkers and maximizing drug-loading efficiency against drug-resistant cancer in vitro. Our research advances the understanding of molecular systems by exploring species evolution via the structural dynamics of polymer folding. Additionally, adaptive synthesis enables controlled, sequential folding of synthetic polymers, with the potential to mimic protein functions.
Ladattava julkaisu This is an electronic reprint of the original article. |  |
Julkaisussa olevat rahoitustiedot:
We are grateful for the financial support from the Sigrid Jusélius Foundation (Senior Researcher Fellowship for J.L.) and the Academy of Finland (decision no. 318524, project funding for J.L.)
