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Issue 89, 2017
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Characterization of protein adsorption on stretched polyurethane nanofibers prepared by electrospinning

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Abstract

Conformation and activity control of proteins adsorbed on certain material surfaces enables the development of numerous high-performance applications. Herein, we examined the relationship between the diameter (surface shape) of polyurethane (PU) nanofibers and the conformation/activity of proteins adsorbed thereon, showing that hard segments align linearly in the long-axis direction when the PU structure is changed from random-segment to stretched nanofibers. Moreover, we revealed that the clustering of hydrophobic hard PU segments and protein adsorption are caused by hydrophobic interactions. Proteins adsorbed on thick nanofibers (diameter = 950 nm) showed decreased activity due to large conformational changes, whereas those adsorbed on thin nanofibers (diameter = 480 nm) retained a close-to-natural shape and thus showed relatively high activity, confirming that the shape of PU nanofiber surface affects the conformation and activity of proteins adsorbed thereon.

Graphical abstract: Characterization of protein adsorption on stretched polyurethane nanofibers prepared by electrospinning

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Publication details

The article was received on 30 Oct 2017, accepted on 08 Dec 2017 and first published on 15 Dec 2017


Article type: Paper
DOI: 10.1039/C7RA11942A
RSC Adv., 2017,7, 56484-56488
  • Open access: Creative Commons BY license
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    Characterization of protein adsorption on stretched polyurethane nanofibers prepared by electrospinning

    Y. Morita, H. Sakamoto and S. Suye, RSC Adv., 2017, 7, 56484
    DOI: 10.1039/C7RA11942A

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