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Surface modification of bacterial magnetic nanoparticles using artificial polypeptides consisting of a repeated asparagine-serine dipeptide and a transmembrane peptide

Published online by Cambridge University Press:  03 September 2012

Toru Honda
Affiliation:
Institute of Engineering, Tokyo University of Agriculture and Technology, 2-24-16, Nakacho, Koganei, 184-8588, Japan
Tomoko Yoshino
Affiliation:
Institute of Engineering, Tokyo University of Agriculture and Technology, 2-24-16, Nakacho, Koganei, 184-8588, Japan
Tsuyoshi Tanaka
Affiliation:
Institute of Engineering, Tokyo University of Agriculture and Technology, 2-24-16, Nakacho, Koganei, 184-8588, Japan
Tadashi Matsunaga
Affiliation:
Institute of Engineering, Tokyo University of Agriculture and Technology, 2-24-16, Nakacho, Koganei, 184-8588, Japan
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Abstract

Surface modification is an important part of fabricating nanoparticles with specific properties and functions. We have designed a dipeptide, which we call NS polypeptide, that consists of four asparagine (N) residues and one serine (S) residue, as a molecule for nanoparticle surface modification. Surface modification of magnetic nanoparticles with the NS polypeptide results in reduction of particle-particle and particle-cell interactions. Here, we describe the surface modification and functionalization of bacterial magnetic particles (BacMPs) by spontaneous integration of temporin L conjugated to NS polypeptide. BacMP membranes were modified temporin L. Furthermore, peptide-modified BacMPs showed high dispersibility in aqueous solution compared to unmodified BacMPs. This surface modification technique may represent a new strategy for reducing non-specific binding of nanoparticles to proteins or cells for use in a variety of protein- or cell-associated applications.

Type
Articles
Copyright
Copyright © Materials Research Society 2012

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