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• W2202760431 abstract "Protein-encapsulated fibermats are an attractive platform for protein-based bioactive materials. However, the choice of methods is still limited and not applicable to a wide range of proteins. In this study, we studied new polymeric materials for constructing protein-encapsulated fibermats, in which protein molecules are encapsulated within the nanofibers of fibermats without causing deleterious changes to protein structure or function. We constructed a protein-encapsulated fibermat using the poly(γ-glutamate) (PGA)/(3-glycidyloxypropyl)-trimethoxysilane (GPTMS) hybrid as a precursor for electrospinning. Because the PGA/GPTMS hybrid is water-soluble, protein molecules can be added to the precursor in an aqueous solution, significantly enhancing protein stability. Polycondensation during electrospinning (in-flight polycondensation) makes the obtained fibermats water-insoluble, which stabilizes the fibermat structure such that it is resistant to degradation in aqueous buffer. The molecular structure of the PGA/GPTMS hybrid gives rise to unique molecular permeability, which alters the selectivity and specificity of biochemical reactions involving the encapsulated enzymes; lower molecular-weight (MW) substrates can permeate the nanofibers, promoting enzyme activity, but higher MW substrates such as inhibitor peptides cannot permeate the nanofibers, suppressing enzyme activity. We present an effective method of encapsulating bioactive molecules while maintaining their structure and function, increasing the versatility of electrospun fibermats for constructing various bioactive materials." @default.
• W2202760431 created "2016-06-24" @default.
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• W2202760431 date "2015-12-31" @default.
• W2202760431 modified "2023-10-14" @default.
• W2202760431 title "Construction and Characterization of Protein-Encapsulated Electrospun Fibermats Prepared from a Silica/Poly(γ-glutamate) Hybrid" @default.
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• W2202760431 doi "https://doi.org/10.1021/acs.langmuir.5b02862" @default.
• W2202760431 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26681447" @default.
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