Protein surface recognition by synthetic receptors based on a tetraphenylporphyrin scaffold

Rishi K. Jain, Andrew Hamilton

Research output: Contribution to journalArticle

Abstract

(matrix presented) Receptors based on a tetraphenylporphyrin scaffold bearing different charged and hydrophobic groups have been synthesized. The interactions of these with horse heart cytochrome c were studied by fluorescence spectroscopy. Receptor 4 was identified to be the strongest synthetic receptor (K d = 20 nM) for cytochrome c. The differences in affinity among the receptors reflected a dependence on the number of anionic and hydrophobic groups.

Original languageEnglish (US)
Pages (from-to)1721-1723
Number of pages3
JournalOrganic Letters
Volume2
Issue number12
StatePublished - Jun 15 2000

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Artificial Receptors
Cytochromes c
Scaffolds
Membrane Proteins
Bearings (structural)
proteins
cytochromes
Fluorescence Spectrometry
Fluorescence spectroscopy
Horses
horses
affinity
fluorescence
tetraphenylporphyrin
matrices
spectroscopy
interactions

ASJC Scopus subject areas

  • Molecular Medicine

Cite this

Protein surface recognition by synthetic receptors based on a tetraphenylporphyrin scaffold. / Jain, Rishi K.; Hamilton, Andrew.

In: Organic Letters, Vol. 2, No. 12, 15.06.2000, p. 1721-1723.

Research output: Contribution to journalArticle

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