Protein Nanoparticle Formation Using a Circularly Permuted α-Helix-Rich Trimeric Protein

Norifumi Kawakami, Hiroki Kondo, Masayuki Muramatsu, Kenji Miyamoto

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

We here report the production of highly spherical protein nanoparticles based on the domain-swapping oligomerization of a circularly permuted trimeric protein, major histocompatibility complex (MHC) class II associated chaperonin. The size distribution of the nanoparticles can be adjusted to between 40 and 100 nm in diameter, and thus, these particles are suitable as drug carriers following purification under basic conditions. Our approach involves no harsh treatments and could provide an alternative approach for protein nanoparticle formation.

Original languageEnglish
Pages (from-to)336-340
Number of pages5
JournalBioconjugate Chemistry
Volume28
Issue number2
DOIs
Publication statusPublished - 2017 Feb 15

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Nanoparticles
Proteins
Chaperonins
Oligomerization
Drug Carriers
Major Histocompatibility Complex
Purification
Therapeutics

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biomedical Engineering
  • Pharmacology
  • Pharmaceutical Science
  • Organic Chemistry

Cite this

Protein Nanoparticle Formation Using a Circularly Permuted α-Helix-Rich Trimeric Protein. / Kawakami, Norifumi; Kondo, Hiroki; Muramatsu, Masayuki; Miyamoto, Kenji.

In: Bioconjugate Chemistry, Vol. 28, No. 2, 15.02.2017, p. 336-340.

Research output: Contribution to journalArticle

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