Modification of porous protein crystals in development of biohybrid materials

Tomomi Koshiyama, Naomi Kawaba, Tatsuo Hikage, Masanobu Shirai, Yuki Miura, Cheng Yuan Huang, Koichiro Tanaka, Yoshihito Watanabe, Takafumi Ueno

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Protein assemblies have attracted increasing attention for construction of biohybrid materials. Protein crystals can also be regarded as solid protein assemblies. The present work demonstrates that protein crystals can be employed as porous biomaterials by site-specific modifications of the crystals of recombinant sperm whale myoglobin mutants. The myoglobin crystals of space group P6 provide hexagonal pores consisting of the building blocks of six Mb molecules, which form a pore with a diameter of 40 Å. On the basis of the lattice structure of the Mb crystals, we have selected appropriate residues located on the surface of the pores for replacement with cysteine. This enables modification of the pore surface via coupling with maleimide derivatives. We have succeeded in crystallizing the modified Mb mutants, retaining the P6 lattice, and consistently aligning nanosized functional molecules such as fluorescein, eosin, and Ru(bpy)3 into the hexagonal pores of the Mb crystals. Our strategy for site-specific modification of protein crystal pores is applicable to various protein crystals with porous structures. We believe that modified porous protein crystals will provide attractive candidates for novel solid materials in nanotechnology applications.

Original languageEnglish
Pages (from-to)264-269
Number of pages6
JournalBioconjugate Chemistry
Volume21
Issue number2
DOIs
Publication statusPublished - Feb 17 2010

Fingerprint

Proteins
Crystals
Myoglobin
Sperm Whale
Porins
Nanotechnology
Biocompatible Materials
Eosine Yellowish-(YS)
Fluorescein
Cysteine
Molecules
Biomaterials
Crystal lattices
Derivatives

All Science Journal Classification (ASJC) codes

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

Cite this

Koshiyama, T., Kawaba, N., Hikage, T., Shirai, M., Miura, Y., Huang, C. Y., ... Ueno, T. (2010). Modification of porous protein crystals in development of biohybrid materials. Bioconjugate Chemistry, 21(2), 264-269. https://doi.org/10.1021/bc9003052

Modification of porous protein crystals in development of biohybrid materials. / Koshiyama, Tomomi; Kawaba, Naomi; Hikage, Tatsuo; Shirai, Masanobu; Miura, Yuki; Huang, Cheng Yuan; Tanaka, Koichiro; Watanabe, Yoshihito; Ueno, Takafumi.

In: Bioconjugate Chemistry, Vol. 21, No. 2, 17.02.2010, p. 264-269.

Research output: Contribution to journalArticle

Koshiyama, T, Kawaba, N, Hikage, T, Shirai, M, Miura, Y, Huang, CY, Tanaka, K, Watanabe, Y & Ueno, T 2010, 'Modification of porous protein crystals in development of biohybrid materials', Bioconjugate Chemistry, vol. 21, no. 2, pp. 264-269. https://doi.org/10.1021/bc9003052
Koshiyama T, Kawaba N, Hikage T, Shirai M, Miura Y, Huang CY et al. Modification of porous protein crystals in development of biohybrid materials. Bioconjugate Chemistry. 2010 Feb 17;21(2):264-269. https://doi.org/10.1021/bc9003052
Koshiyama, Tomomi ; Kawaba, Naomi ; Hikage, Tatsuo ; Shirai, Masanobu ; Miura, Yuki ; Huang, Cheng Yuan ; Tanaka, Koichiro ; Watanabe, Yoshihito ; Ueno, Takafumi. / Modification of porous protein crystals in development of biohybrid materials. In: Bioconjugate Chemistry. 2010 ; Vol. 21, No. 2. pp. 264-269.
@article{31e2c043ac104f908d236dd59e82dedd,
title = "Modification of porous protein crystals in development of biohybrid materials",
abstract = "Protein assemblies have attracted increasing attention for construction of biohybrid materials. Protein crystals can also be regarded as solid protein assemblies. The present work demonstrates that protein crystals can be employed as porous biomaterials by site-specific modifications of the crystals of recombinant sperm whale myoglobin mutants. The myoglobin crystals of space group P6 provide hexagonal pores consisting of the building blocks of six Mb molecules, which form a pore with a diameter of 40 {\AA}. On the basis of the lattice structure of the Mb crystals, we have selected appropriate residues located on the surface of the pores for replacement with cysteine. This enables modification of the pore surface via coupling with maleimide derivatives. We have succeeded in crystallizing the modified Mb mutants, retaining the P6 lattice, and consistently aligning nanosized functional molecules such as fluorescein, eosin, and Ru(bpy)3 into the hexagonal pores of the Mb crystals. Our strategy for site-specific modification of protein crystal pores is applicable to various protein crystals with porous structures. We believe that modified porous protein crystals will provide attractive candidates for novel solid materials in nanotechnology applications.",
author = "Tomomi Koshiyama and Naomi Kawaba and Tatsuo Hikage and Masanobu Shirai and Yuki Miura and Huang, {Cheng Yuan} and Koichiro Tanaka and Yoshihito Watanabe and Takafumi Ueno",
year = "2010",
month = "2",
day = "17",
doi = "10.1021/bc9003052",
language = "English",
volume = "21",
pages = "264--269",
journal = "Bioconjugate Chemistry",
issn = "1043-1802",
publisher = "American Chemical Society",
number = "2",

}

TY - JOUR

T1 - Modification of porous protein crystals in development of biohybrid materials

AU - Koshiyama, Tomomi

AU - Kawaba, Naomi

AU - Hikage, Tatsuo

AU - Shirai, Masanobu

AU - Miura, Yuki

AU - Huang, Cheng Yuan

AU - Tanaka, Koichiro

AU - Watanabe, Yoshihito

AU - Ueno, Takafumi

PY - 2010/2/17

Y1 - 2010/2/17

N2 - Protein assemblies have attracted increasing attention for construction of biohybrid materials. Protein crystals can also be regarded as solid protein assemblies. The present work demonstrates that protein crystals can be employed as porous biomaterials by site-specific modifications of the crystals of recombinant sperm whale myoglobin mutants. The myoglobin crystals of space group P6 provide hexagonal pores consisting of the building blocks of six Mb molecules, which form a pore with a diameter of 40 Å. On the basis of the lattice structure of the Mb crystals, we have selected appropriate residues located on the surface of the pores for replacement with cysteine. This enables modification of the pore surface via coupling with maleimide derivatives. We have succeeded in crystallizing the modified Mb mutants, retaining the P6 lattice, and consistently aligning nanosized functional molecules such as fluorescein, eosin, and Ru(bpy)3 into the hexagonal pores of the Mb crystals. Our strategy for site-specific modification of protein crystal pores is applicable to various protein crystals with porous structures. We believe that modified porous protein crystals will provide attractive candidates for novel solid materials in nanotechnology applications.

AB - Protein assemblies have attracted increasing attention for construction of biohybrid materials. Protein crystals can also be regarded as solid protein assemblies. The present work demonstrates that protein crystals can be employed as porous biomaterials by site-specific modifications of the crystals of recombinant sperm whale myoglobin mutants. The myoglobin crystals of space group P6 provide hexagonal pores consisting of the building blocks of six Mb molecules, which form a pore with a diameter of 40 Å. On the basis of the lattice structure of the Mb crystals, we have selected appropriate residues located on the surface of the pores for replacement with cysteine. This enables modification of the pore surface via coupling with maleimide derivatives. We have succeeded in crystallizing the modified Mb mutants, retaining the P6 lattice, and consistently aligning nanosized functional molecules such as fluorescein, eosin, and Ru(bpy)3 into the hexagonal pores of the Mb crystals. Our strategy for site-specific modification of protein crystal pores is applicable to various protein crystals with porous structures. We believe that modified porous protein crystals will provide attractive candidates for novel solid materials in nanotechnology applications.

UR - http://www.scopus.com/inward/record.url?scp=77049097935&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77049097935&partnerID=8YFLogxK

U2 - 10.1021/bc9003052

DO - 10.1021/bc9003052

M3 - Article

C2 - 20099839

AN - SCOPUS:77049097935

VL - 21

SP - 264

EP - 269

JO - Bioconjugate Chemistry

JF - Bioconjugate Chemistry

SN - 1043-1802

IS - 2

ER -