Enantioselective regulation of a metal complex in reversible binding to serum albumin: dynamic helicity inversion signalled by circularly polarised luminescence

文献情報

出版日 2008-09-10

DOI 10.1039/B810978H

インパクトファクター 6.222

著者

Craig P. Montgomery, Elizabeth J. New, David Parker, Robert D. Peacock

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要旨

The helicity of the (SSS)-Δ enantiomer of a terbium and europium(III) complex is inverted on reversible binding to ‘drug site II’ of serum albumin, signalled by a switch in its circularly polarised emission; no such behaviour occurs with the (RRR)-Λ complexes, thereby defining a unique chiroptical probe of albumin binding.

掲載誌

Chemical Communications

CiteScore: 8.6

自己引用率: 4.7%

年間論文数: 2458

ChemComm publishes urgent research which is of outstanding significance and interest to experts in the field, while also appealing to the journal’s broad chemistry readership. Our communication format is ideally suited to short, urgent studies that are of such importance that they require accelerated publication. Our scope covers all topics in chemistry, and research at the interface of chemistry and other disciplines (such as materials science, nanoscience, physics, engineering and biology) where there is a significant novelty in the chemistry aspects. Major topic areas covered include: Analytical Chemistry Catalysis Chemical Biology and medicinal chemistry Computational Chemistry and Machine Learning Energy and sustainable chemistry Environmental Chemistry Green Chemistry Inorganic Chemistry Materials Chemistry Nanoscience Organic Chemistry Physical Chemistry Polymer Chemistry Supramolecular Chemistry

Enantioselective regulation of a metal complex in reversible binding to serum albumin: dynamic helicity inversion signalled by circularly polarised luminescence

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