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Correlating solution binding and ESI-MS stabilities by incorporating solvation effects in a confined cucurbit[8]uril system.

Abstract:

The high-throughput characterization of solution binding equilibria is essential in biomedical research such as drug design as well as in material applications of synthetic systems in which reversible binding interactions play critical roles. Although isothermal titration calorimetry (ITC) has been widely employed for describing such binding events, factors such as speed, concentration, and sample complexity would principally favor a mass spectrometry approach. Here, we show a link between IT...

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Publication status:
Published

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Publisher copy:
10.1021/jp102933h

Authors


Journal:
The journal of physical chemistry. B
Volume:
114
Issue:
26
Pages:
8606-8615
Publication date:
2010-07-05
DOI:
EISSN:
1520-5207
ISSN:
1520-6106
URN:
uuid:63e1392e-aadf-4fb9-8350-c077b3027467
Source identifiers:
60302
Local pid:
pubs:60302

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