Chaperone/Polymer Complexation of Protein-Based Fluorescent Nanoclusters against Silica Encapsulation-Induced Physicochemical Stresses

Silica encapsulation under ambient conditions is commonly used to shield protein-based nanosystems from chemical stress. However, encapsulation-induced photo- and structural instabilities at elevated temperatures have been overlooked. Using bovine serum albumin-capped fluorescent gold nanoclusters (...

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Vydáno v:Biomacromolecules Ročník 25; číslo 10; s. 6515
Hlavní autoři: Akbarian, Mohsen, Chen, I-Ni, Lu, Pei-Hsuan, Do, Quynh-Trang, Tzeng, Shun-Fen, Chou, Ho-Hsuan, Chen, Shu-Hui
Médium: Journal Article
Jazyk:angličtina
Vydáno: United States 14.10.2024
Témata:
Acrylic Resins - chemistry
alpha-Crystallins - chemistry
Animals
Cattle
Fluorescent Dyes - chemistry
Gold - chemistry
Humans
Metal Nanoparticles - chemistry
Molecular Chaperones - chemistry
Serum Albumin, Bovine - chemistry
Silicon Dioxide - chemistry
ISSN:1526-4602, 1526-4602
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Shrnutí:Silica encapsulation under ambient conditions is commonly used to shield protein-based nanosystems from chemical stress. However, encapsulation-induced photo- and structural instabilities at elevated temperatures have been overlooked. Using bovine serum albumin-capped fluorescent gold nanoclusters (BSA-AuNCs) as a model, we demonstrated that chaperone/polymer layer-by-layer complexation can stabilize the template to resist encapsulation-induced fragmentation/reorganization and emission increases at 37 °C or higher temperatures. We first wrapped BSA-AuNCs with α-crystallin chaperones (α-Crys) to gain the highest thermal stability at a 1:50 molar ratio and then enfolded BSA-AuNC/α-Crys with thermoresponsive poly- -isopropylacrylamide (PNIPAM) at 60 °C to shield silica interaction and increase the chaperone-client protein accessibility. The resulting BSA-AuNC/α-Crys/PNIPAM (BαP) was encapsulated by a sol-gel process to yield BαP-Si (∼80 ± 4.5 nm), which exhibited excellent structural integrity and photostability against chemical and thermal stresses. Moreover, targeted BαP-Si demonstrated prolonged fluorescence stability for cancer cell imaging. This template stabilization strategy for silica encapsulation is biocompatible and applicable to other protein-based nanosystems.
Bibliografie:ObjectType-Article-1
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ISSN:1526-4602
1526-4602
DOI:10.1021/acs.biomac.4c00689