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

Toru Honda, Tomoko Yoshino, Tsuyoshi Tanaka, Tadashi Matsunaga

Research output: Chapter in Book/Report/Conference proceedingConference contribution

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.

Original languageEnglish
Title of host publicationMolecules to Materials - Multiscale Interfacial Phenomena in Biological and Bio-Inspired Materials
Pages7-12
Number of pages6
Volume1464
DOIs
Publication statusPublished - 2012
Externally publishedYes
Event2012 MRS Spring Meeting - San Francisco, CA, United States
Duration: 2012 Apr 92012 Apr 13

Other

Other2012 MRS Spring Meeting
CountryUnited States
CitySan Francisco, CA
Period12/4/912/4/13

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ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics
  • Mechanics of Materials
  • Mechanical Engineering

Cite this

Honda, T., Yoshino, T., Tanaka, T., & Matsunaga, T. (2012). Surface modification of bacterial magnetic nanoparticles using artificial polypeptides consisting of a repeated asparagine-serine dipeptide and a transmembrane peptide. In Molecules to Materials - Multiscale Interfacial Phenomena in Biological and Bio-Inspired Materials (Vol. 1464, pp. 7-12) https://doi.org/10.1557/opl.2012.1468