Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 539-545 |
| Number of pages | 6 |
| Journal | Macromolecular bioscience |
| Volume | 10 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 2010 |
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Keywords
- PROTEINS
- self-assembly supramolecular structures
- Nanotechnology
- bioengineering
- METIS-273734
- IR-77546
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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 journal › Article › Academic › peer-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
U2 - 10.1002/mabi.201000030
DO - 10.1002/mabi.201000030
M3 - Article
VL - 10
SP - 539
EP - 545
JO - Macromolecular bioscience
JF - Macromolecular bioscience
SN - 1616-5187
IS - 5
ER -