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Issue 89, 2017

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

Article information


Submitted
30 Oct 2017
Accepted
08 Dec 2017
First published
15 Dec 2017

This article is Open Access

RSC Adv., 2017,7, 56484-56488
Article type
Paper

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

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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