Cellular uptake of highly-functionalized ruthenium(II) tris-bipyridine protein-surface mimetics

Susan J. Turrell; Maria H. Filby; Adrian Whitehouse; Andrew J. Wilson

doi:10.1016/j.bmcl.2011.12.007

Cellular uptake of highly-functionalized ruthenium(II) tris-bipyridine protein-surface mimetics

Susan J. Turrell
, Maria H. Filby
, Adrian Whitehouse^*
, Andrew J. Wilson

^*Corresponding author for this work

Chemistry

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

6 Citations (Scopus)

Abstract

This manuscript describes cell-uptake studies with HEK 293T cells on a series of ruthenium complexes shown previously to act as receptors for protein surface recognition and was motivated by a desire to establish if these receptors represent suitable templates for further elaboration as inhibitors of protein-protein interactions. The results illustrate that large (>3000 Da) highly functionalized anionic ruthenium complexes are efficiently transfected via endocytosis to lysosomes with negligible toxicity.

Original language	English
Pages (from-to)	985-988
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	22
Issue number	2
DOIs	https://doi.org/10.1016/j.bmcl.2011.12.007
Publication status	Published - 15 Jan 2012

Bibliographical note

Funding Information:
This work was supported by the European Research Council [ERC-StG-240324] the EPSRC [EP/F039069] and the BBSRC (DTG PhD studentship). The authors wish to thank Amy Barker for Sedimentation Velocity Analytical Ultracentrifugation (facility funded by The Wellcome Trust) and the Wolfson Analytical Facility (University of Leeds) for Zeta Potential measurements.

Keywords

Cellular uptake
Protein-surface receptors
Ruthenium complexes

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Pharmaceutical Science
Drug Discovery
Clinical Biochemistry
Organic Chemistry

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10.1016/j.bmcl.2011.12.007

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title = "Cellular uptake of highly-functionalized ruthenium(II) tris-bipyridine protein-surface mimetics",

abstract = "This manuscript describes cell-uptake studies with HEK 293T cells on a series of ruthenium complexes shown previously to act as receptors for protein surface recognition and was motivated by a desire to establish if these receptors represent suitable templates for further elaboration as inhibitors of protein-protein interactions. The results illustrate that large (>3000 Da) highly functionalized anionic ruthenium complexes are efficiently transfected via endocytosis to lysosomes with negligible toxicity.",

keywords = "Cellular uptake, Protein-surface receptors, Ruthenium complexes",

author = "Turrell, \{Susan J.\} and Filby, \{Maria H.\} and Adrian Whitehouse and Wilson, \{Andrew J.\}",

note = "Funding Information: This work was supported by the European Research Council [ERC-StG-240324] the EPSRC [EP/F039069] and the BBSRC (DTG PhD studentship). The authors wish to thank Amy Barker for Sedimentation Velocity Analytical Ultracentrifugation (facility funded by The Wellcome Trust) and the Wolfson Analytical Facility (University of Leeds) for Zeta Potential measurements. ",

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AU - Turrell, Susan J.

AU - Filby, Maria H.

AU - Whitehouse, Adrian

AU - Wilson, Andrew J.

N1 - Funding Information: This work was supported by the European Research Council [ERC-StG-240324] the EPSRC [EP/F039069] and the BBSRC (DTG PhD studentship). The authors wish to thank Amy Barker for Sedimentation Velocity Analytical Ultracentrifugation (facility funded by The Wellcome Trust) and the Wolfson Analytical Facility (University of Leeds) for Zeta Potential measurements.

PY - 2012/1/15

Y1 - 2012/1/15

N2 - This manuscript describes cell-uptake studies with HEK 293T cells on a series of ruthenium complexes shown previously to act as receptors for protein surface recognition and was motivated by a desire to establish if these receptors represent suitable templates for further elaboration as inhibitors of protein-protein interactions. The results illustrate that large (>3000 Da) highly functionalized anionic ruthenium complexes are efficiently transfected via endocytosis to lysosomes with negligible toxicity.

AB - This manuscript describes cell-uptake studies with HEK 293T cells on a series of ruthenium complexes shown previously to act as receptors for protein surface recognition and was motivated by a desire to establish if these receptors represent suitable templates for further elaboration as inhibitors of protein-protein interactions. The results illustrate that large (>3000 Da) highly functionalized anionic ruthenium complexes are efficiently transfected via endocytosis to lysosomes with negligible toxicity.

KW - Cellular uptake

KW - Protein-surface receptors

KW - Ruthenium complexes

UR - https://www.scopus.com/pages/publications/84855648470

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DO - 10.1016/j.bmcl.2011.12.007

M3 - Article

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AN - SCOPUS:84855648470

SN - 0960-894X

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JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

IS - 2

ER -

Cellular uptake of highly-functionalized ruthenium(II) tris-bipyridine protein-surface mimetics

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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