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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Bibliographic Details
Published in:	Biomacromolecules Vol. 25; no. 10; p. 6515
Main Authors:	Akbarian, Mohsen, Chen, I-Ni, Lu, Pei-Hsuan, Do, Quynh-Trang, Tzeng, Shun-Fen, Chou, Ho-Hsuan, Chen, Shu-Hui
Format:	Journal Article
Language:	English
Published:	United States 14.10.2024
Subjects:	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
Online Access:	Get more information
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Summary:	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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1526-4602 1526-4602
DOI:	10.1021/acs.biomac.4c00689