A chiral probe for the acute phase proteins alpha-1-acid glycoprotein and alpha-1-antitrypsin based on europium luminescence

Rachel Carr; Lorenzo Di Bari; Samuele Lo Piano; David Parker; Robert D. Peacock; John M. Sanderson

doi:10.1039/c2dt30143a

A chiral probe for the acute phase proteins alpha-1-acid glycoprotein and alpha-1-antitrypsin based on europium luminescence

Rachel Carr
, Lorenzo Di Bari
, Samuele Lo Piano
, David Parker^*
, Robert D. Peacock
, John M. Sanderson

^*Corresponding author for this work

Department of Chemistry

Research output: Contribution to journal › Journal article › peer-review

48 Citations (Scopus)

Abstract

Reversible and selective binding of a dynamically racemic europium(iii) complex to α₁-acid glycoprotein and α₁- antitrypsin is characterised by a significant change in the europium total emission spectral fingerprint and the switching on of a large circularly polarised luminescence (CPL) signal from the metal centre. Observation of an induced CD into the ligand chromophore in the presence of α₁- AGP allows a structure for the protein-bound complex to be postulated. A direct determination of elevated α₁-AGP levels in human serum was achieved by monitoring changes in the intensity ratio of Eu emission bands.

Original language	English
Pages (from-to)	13154-13158
Number of pages	5
Journal	Dalton Transactions
Volume	41
Issue number	42
Early online date	14 Feb 2012
DOIs	https://doi.org/10.1039/c2dt30143a
Publication status	Published - 10 Oct 2012

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10.1039/c2dt30143a

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@article{12dc8e452f524794a486393b73bee97b,

title = "A chiral probe for the acute phase proteins alpha-1-acid glycoprotein and alpha-1-antitrypsin based on europium luminescence",

abstract = "Reversible and selective binding of a dynamically racemic europium(iii) complex to α1-acid glycoprotein and α1- antitrypsin is characterised by a significant change in the europium total emission spectral fingerprint and the switching on of a large circularly polarised luminescence (CPL) signal from the metal centre. Observation of an induced CD into the ligand chromophore in the presence of α1- AGP allows a structure for the protein-bound complex to be postulated. A direct determination of elevated α1-AGP levels in human serum was achieved by monitoring changes in the intensity ratio of Eu emission bands.",

author = "Rachel Carr and \{Di Bari\}, Lorenzo and \{Lo Piano\}, Samuele and David Parker and Peacock, \{Robert D.\} and Sanderson, \{John M.\}",

note = "We thank EPSRC and the ERC (FCC, 266084) for support. Publisher Copyright: {\textcopyright} The Royal Society of Chemistry 2012",

year = "2012",

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doi = "10.1039/c2dt30143a",

language = "English",

volume = "41",

pages = "13154--13158",

journal = "Dalton Transactions",

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TY - JOUR

T1 - A chiral probe for the acute phase proteins alpha-1-acid glycoprotein and alpha-1-antitrypsin based on europium luminescence

AU - Carr, Rachel

AU - Di Bari, Lorenzo

AU - Lo Piano, Samuele

AU - Parker, David

AU - Peacock, Robert D.

AU - Sanderson, John M.

PY - 2012/10/10

Y1 - 2012/10/10

N2 - Reversible and selective binding of a dynamically racemic europium(iii) complex to α1-acid glycoprotein and α1- antitrypsin is characterised by a significant change in the europium total emission spectral fingerprint and the switching on of a large circularly polarised luminescence (CPL) signal from the metal centre. Observation of an induced CD into the ligand chromophore in the presence of α1- AGP allows a structure for the protein-bound complex to be postulated. A direct determination of elevated α1-AGP levels in human serum was achieved by monitoring changes in the intensity ratio of Eu emission bands.

AB - Reversible and selective binding of a dynamically racemic europium(iii) complex to α1-acid glycoprotein and α1- antitrypsin is characterised by a significant change in the europium total emission spectral fingerprint and the switching on of a large circularly polarised luminescence (CPL) signal from the metal centre. Observation of an induced CD into the ligand chromophore in the presence of α1- AGP allows a structure for the protein-bound complex to be postulated. A direct determination of elevated α1-AGP levels in human serum was achieved by monitoring changes in the intensity ratio of Eu emission bands.

UR - https://www.scopus.com/pages/publications/84867378977

UR - https://pubs.rsc.org/en/content/articlelanding/2012/dt/c2dt30143a

U2 - 10.1039/c2dt30143a

DO - 10.1039/c2dt30143a

M3 - Journal article

C2 - 23023320

AN - SCOPUS:84867378977

SN - 1477-9226

VL - 41

SP - 13154

EP - 13158

JO - Dalton Transactions

JF - Dalton Transactions

IS - 42

ER -

A chiral probe for the acute phase proteins alpha-1-acid glycoprotein and alpha-1-antitrypsin based on europium luminescence

Abstract

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