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- W3128895413 abstract "Bio-hybrid materials have received a lot of attention in view of their bio-mimicking nature. One such biomimetic material with catalytic activity are the protein derived floral nanohybrid. Copper phosphate coordinated flakes can be curated to distinct floral morphology using proteins. Structurally two different proteins with similar size and with no known enzymatic activity are used to evaluate the role of protein structure and morphology, on the structure-activity relationship of the developed hybrid nanoflowers. Globular protein BSA and bacterial microcompartment domain protein PduBB′ are selected. PduBB′ because of self-assembling nature forms extended sheets, whereas BSA lacks specific assembly. The developed hybrid NFs differ in their morphology and also in their mimicry as a biological catalyst. The present investigation highlights the importance of the quaternary structure of proteins in tailoring the structure and function of the h-NFs. The results in this manuscript will motivate and guide designing, engineering and selection of glue material for fabricating biomacromolecule derived biohybrid material to mimic natural enzymes of potential industrial application." @default.
- W3128895413 created "2021-02-15" @default.
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- W3128895413 date "2021-04-01" @default.
- W3128895413 modified "2023-10-13" @default.
- W3128895413 title "Protein morphology drives the structure and catalytic activity of bio-inorganic hybrids" @default.
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- W3128895413 doi "https://doi.org/10.1016/j.ijbiomac.2021.01.217" @default.
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