4.7 Article

Poly(ε-caprolactone) (PCL)-polymeric micelle hybrid sheets for the incorporation and release of hydrophilic proteins

Journal

COLLOIDS AND SURFACES B-BIOINTERFACES
Volume 127, Issue -, Pages 292-299

Publisher

ELSEVIER
DOI: 10.1016/j.colsurfb.2015.01.028

Keywords

Sheet; Polymeric micelle; Protein; Sustained release; Fractal analysis

Funding

  1. Ministry of Education, Culture, Sports, Science, and Technology of Japan (MEXT) [22700490]
  2. Grants-in-Aid for Scientific Research [22700490] Funding Source: KAKEN

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Sheets have several advantages over conventional gel- or particle-type drug carriers. Sheets have several notable attributes: sheets' size and shape are easily adjustable, sheets are highly accessible in surgery, and sheets have a large contact area relative to drug-targeting sites. However, it is difficult to incorporate hydrophilic proteins into hydrophobic sheets and to release the proteins over the long term in a sustained manner. In the present study, we show that poly(epsilon-caprolactone) (PCL)-polymeric micelle hybrid sheets can be used for the incorporation and release of hydrophilic proteins. Polymeric micelles (i.e., spaces that can incorporate hydrophilic compounds) are, in this study, uniformly dispersed in hydrophobic and biocompatible biomaterial sheet. We have clarified that the composition of block copolymer, methoxy-terminated poly(ethylene glycol)-block-poly(epsilon-caprolactone) (CH3O-PEG-b-PCL), can affect two variables: the stability of w/o emulsion and the release properties of the resulting sheets, by means of visual qualitative observations, newly developed quantitative analyses (advanced fractal analysis, advanced FD) based on deviation of the fractal dimension (FD), and release experiments. We clarified that the release behavior of BSA was affected by the composition of the block copolymers and the resulting emulsion. The results obtained in this paper show that the hydrophobic sheets in which polymeric micelles providing hydrophilic spaces were dispersed could be an effective platform for incorporating and releasing hydrophilic proteins. (C) 2015 Elsevier B.V. All rights reserved.

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