Controlled encapsulation of multiple proteins in virus capsids

Inge J. Minten; Linda J.A. Hendriks; Roeland J.M. Nolte; Jeroen Johannes Lambertus Maria Cornelissen

doi:10.1021/ja907843s

Controlled encapsulation of multiple proteins in virus capsids

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

Research output: Contribution to journal › Article › Academic › peer-review

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Abstract

Multiple proteins can be bound within the Cowpea Chlorotic Mottle Virus capsid shell in an efficient and controlled manner by using heterodimeric coiled-coil peptide oligomers. Through genetic modification, these oligomers can be attached to the capsid protein and an enhanced green fluorescent protein (EGFP). In this way, the capsid proteins can be noncovalently bound to EGFP prior to the induction of the capsid assembly. Up to 15 EGFP proteins can be encapsulated per capsid in a controlled and efficient manner

Original language	Undefined
Pages (from-to)	17771-17773
Number of pages	3
Journal	Journal of the American Chemical Society
Volume	131
Issue number	49
DOIs	https://doi.org/10.1021/ja907843s
Publication status	Published - 2009

Keywords

IR-77783
METIS-263228

Access to Document

10.1021/ja907843s

Cite this

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title = "Controlled encapsulation of multiple proteins in virus capsids",

abstract = "Multiple proteins can be bound within the Cowpea Chlorotic Mottle Virus capsid shell in an efficient and controlled manner by using heterodimeric coiled-coil peptide oligomers. Through genetic modification, these oligomers can be attached to the capsid protein and an enhanced green fluorescent protein (EGFP). In this way, the capsid proteins can be noncovalently bound to EGFP prior to the induction of the capsid assembly. Up to 15 EGFP proteins can be encapsulated per capsid in a controlled and efficient manner",

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AU - Hendriks, Linda J.A.

AU - Nolte, Roeland J.M.

AU - Cornelissen, Jeroen Johannes Lambertus Maria

PY - 2009

Y1 - 2009

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AB - Multiple proteins can be bound within the Cowpea Chlorotic Mottle Virus capsid shell in an efficient and controlled manner by using heterodimeric coiled-coil peptide oligomers. Through genetic modification, these oligomers can be attached to the capsid protein and an enhanced green fluorescent protein (EGFP). In this way, the capsid proteins can be noncovalently bound to EGFP prior to the induction of the capsid assembly. Up to 15 EGFP proteins can be encapsulated per capsid in a controlled and efficient manner

KW - IR-77783

KW - METIS-263228

U2 - 10.1021/ja907843s

DO - 10.1021/ja907843s

M3 - Article

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