Complex assembly behavior during the encapsulation of green fluorescent protein analogs in virus derived protein capsules

Inge J. Minten, Roeland J.M. Nolte, Jeroen Johannes Lambertus Maria Cornelissen

Research output: Contribution to journalArticleAcademicpeer-review

14 Citations (Scopus)

Abstract

Enzymes encapsulated in nanocontainers are a better model of the conditions inside a living cell than free enzymes in solution. In a first step toward the encapsulation of multiple enzymes inside the cowpea chlorotic mottle virus (CCMV) capsid, enhanced green fluorescent protein (EGFP) was attached to CCMV capsid proteins. The capsid protein–EGFP complex was then co-assembled with wild-type capsid protein (wt CP) in various ratios. At higher complex to wt CP ratios, the number of EGFP per capsid decreased instead of leveling off. We propose that this unexpected behavior is caused by pH-induced disassembly of the capsid protein–EGFP complex as well as by concentration and ratio dependent dimerization of the complex, making it partially unavailable for incorporation into the capsid.
Original languageEnglish
Pages (from-to)539-545
Number of pages6
JournalMacromolecular bioscience
Volume10
Issue number5
DOIs
Publication statusPublished - 2010

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Capsid
Capsid Proteins
Green Fluorescent Proteins
Viruses
Encapsulation
Capsules
Proteins
Bromovirus
Enzymes
Dimerization
Cells
enhanced green fluorescent protein

Keywords

  • PROTEINS
  • self-assembly supramolecular structures
  • Nanotechnology
  • bioengineering
  • METIS-273734
  • IR-77546

Cite this

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title = "Complex assembly behavior during the encapsulation of green fluorescent protein analogs in virus derived protein capsules",
abstract = "Enzymes encapsulated in nanocontainers are a better model of the conditions inside a living cell than free enzymes in solution. In a first step toward the encapsulation of multiple enzymes inside the cowpea chlorotic mottle virus (CCMV) capsid, enhanced green fluorescent protein (EGFP) was attached to CCMV capsid proteins. The capsid protein–EGFP complex was then co-assembled with wild-type capsid protein (wt CP) in various ratios. At higher complex to wt CP ratios, the number of EGFP per capsid decreased instead of leveling off. We propose that this unexpected behavior is caused by pH-induced disassembly of the capsid protein–EGFP complex as well as by concentration and ratio dependent dimerization of the complex, making it partially unavailable for incorporation into the capsid.",
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Complex assembly behavior during the encapsulation of green fluorescent protein analogs in virus derived protein capsules. / Minten, Inge J.; Nolte, Roeland J.M.; Cornelissen, Jeroen Johannes Lambertus Maria.

In: Macromolecular bioscience, Vol. 10, No. 5, 2010, p. 539-545.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Complex assembly behavior during the encapsulation of green fluorescent protein analogs in virus derived protein capsules

AU - Minten, Inge J.

AU - Nolte, Roeland J.M.

AU - Cornelissen, Jeroen Johannes Lambertus Maria

PY - 2010

Y1 - 2010

N2 - Enzymes encapsulated in nanocontainers are a better model of the conditions inside a living cell than free enzymes in solution. In a first step toward the encapsulation of multiple enzymes inside the cowpea chlorotic mottle virus (CCMV) capsid, enhanced green fluorescent protein (EGFP) was attached to CCMV capsid proteins. The capsid protein–EGFP complex was then co-assembled with wild-type capsid protein (wt CP) in various ratios. At higher complex to wt CP ratios, the number of EGFP per capsid decreased instead of leveling off. We propose that this unexpected behavior is caused by pH-induced disassembly of the capsid protein–EGFP complex as well as by concentration and ratio dependent dimerization of the complex, making it partially unavailable for incorporation into the capsid.

AB - Enzymes encapsulated in nanocontainers are a better model of the conditions inside a living cell than free enzymes in solution. In a first step toward the encapsulation of multiple enzymes inside the cowpea chlorotic mottle virus (CCMV) capsid, enhanced green fluorescent protein (EGFP) was attached to CCMV capsid proteins. The capsid protein–EGFP complex was then co-assembled with wild-type capsid protein (wt CP) in various ratios. At higher complex to wt CP ratios, the number of EGFP per capsid decreased instead of leveling off. We propose that this unexpected behavior is caused by pH-induced disassembly of the capsid protein–EGFP complex as well as by concentration and ratio dependent dimerization of the complex, making it partially unavailable for incorporation into the capsid.

KW - PROTEINS

KW - self-assembly supramolecular structures

KW - Nanotechnology

KW - bioengineering

KW - METIS-273734

KW - IR-77546

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DO - 10.1002/mabi.201000030

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