In situ monitoring of protein transfer into nanoscale channels

Pan, Yanxiong; Wang, Xiaoliang; Li, Hui; Ren, Junyu; Zhang, Yin; Jordahl, Drew; Schuster, Iris; Farmakes, Jasmin; Hong, Heedeok; Yang, Zhongyu; Ma, Shengqian

doi:10.1016/j.xcrp.2021.100576

Cited by 14 publications

(8 citation statements)

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“…Beyond hydrogen bonding, hydrophobic interactions may also contribute to the structural change. [27] However, the content of β-sheet from HRP-COF-LZU1 is increased, whereas the content of β-sheet from HRP-RT-COF-1 and HRP-ACOF-1 is decreased, suggesting the HRP conformation in COF-LZU1 is more favorable. the enzyme experienced significant structural alteration upon immobilization within reticular framework, although this structural change is generally not stable in its free form, as evidenced by our previous research that the reticular frameworks could lock this fragile conformation and improve the enzyme stability.…”

Section: Resultsmentioning

confidence: 96%

“…The HRP in different COFs undergoes a similar transition, which implies that a nonspecific hydrogen bond interaction between the enzyme and COF framework is present. Beyond hydrogen bonding, hydrophobic interactions may also contribute to the structural change [27] . However, the content of β‐sheet from HRP‐COF‐LZU1 is increased, whereas the content of β‐sheet from HRP‐RT‐COF‐1 and HRP‐ACOF‐1 is decreased, suggesting the HRP conformation in COF‐LZU1 is more favorable.…”

Section: Resultsmentioning

confidence: 99%

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Insight into Bioactivity of In‐situ Trapped Enzyme‐Covalent‐Organic Frameworks

et al. 2023

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Selecting a suitable support material for enzyme immobilization with excellent biocatalytic activity and stability is a critical aspect in the development of functional biosystems. The highly stable and metal‐free properties of covalent‐organic frameworks (COFs) make them ideal supports for enzyme immobilization. Herein, we constructed three kinds of COFs via a biofriendly and one‐pot synthetic strategy at room temperature in aqueous solution. Among the three developed COFs (COF‐LZU1, RT‐COF‐1 and ACOF‐1), the horseradish peroxidase (HRP)‐incorporated COF‐LZU1 is found to retain the highest activity. Structural analysis reveals that a weakest interaction between the hydrated enzyme and COF‐LZU1, an easiest accessibility by the COF‐LZU1 to the substrate, as well as an optimal conformation of enzyme together promote the bioactivity of HRP‐COF‐LZU1. Furthermore, the COF‐LZU1 is revealed to be a versatile nanoplatform for encapsulating multiple enzymes. The COF‐LZU1 also offers superior protection for the immobilized enzymes under harsh conditions and during recycling. The comprehensive understanding of interfacial interactions of COF host and enzyme guest, the substrate diffusion, as well as the enzyme conformation alteration within COF matrices represents an opportunity to design the ideal biocatalysts and opens a broad range of applications of these nanosystems.

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Section: Resultsmentioning

confidence: 96%

Section: Resultsmentioning

confidence: 99%

Insight into Bioactivity of In‐situ Trapped Enzyme‐Covalent‐Organic Frameworks

et al. 2023

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“…Figure 4F reveals the remarkable catalytic activity of CAT/HCPOS-1 with a rate of 6.0 μM•s -1 , approximately 67% of the activity of the free enzyme (8.9 μM•s -1 ), indicating that the enzyme structure is not significantly disrupted during the immobilization process. The hydrophilic nature of the surface plays a crucial role in maintaining the active conformation of enzymes [60,61] . In the case of HCPOS-1, numerous polar functional groups on the surface impart HCPOS-1 with a hydrophilic surface, as confirmed by water contact angle measurement [Supplementary Figure 18].…”

Section: Resultsmentioning

confidence: 99%

A 3D ordered hierarchical crystalline porous organic salt for large-sized enzyme immobilization

Wang,

Xing,

Zhao

et al. 2024

Chem Synth

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Crystalline porous organic salts (CPOSs) are an emerging class of promising materials with intrinsic highly polar nanoconfined microporosity. However, their single microporous structure greatly hinders their development in the field of catalysis and adsorption. Constructing a hierarchical porous structure can effectively reduce the mass transport resistance, thus expanding the scope of their applications. Herein, we report the synthesis of a three-dimensional (3D) ordered macro-/microporous hierarchical CPOS (HCPOS-1) using a template-assisted approach for the first time. The as-synthesized HCPOS-1 prepared from a polystyrene colloidal crystal template showcases a 3D ordered macroporous structure while also preserving the microporous structure. The 3D ordered macroporous structure in such a hierarchical structure, together with its hydrophilic surface, endows HCPOS-1 with the ability to immobilize large-sized enzymes through physical adsorption under mild conditions. The resulting catalase/HCPOS-1 showcases a high enzyme immobilization capacity and avoids undesired conformational changes of enzymes during the immobilization process, thus exhibiting excellent catalytic activity for the decomposition of hydrogen peroxide.

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“…17). 190 In the time-resolved EPR spectra, different loading profiles were observed among the different channels with different surface charges and hydrophobicity distributions, which depended on the different host–guest interactions, such as electrostatic interaction for a charged channel and hydrophobic interaction for a hydrophobic channel. Even in the same channel, the enzyme orientation changed with time due to the host preference toward each labelled site.…”

Section: Enzyme Conformation and Its Functional Activitymentioning

confidence: 99%