Protein surface recognition by porphyrin-based receptors

Lun K. Tsou, Rishi K. Jain, Andrew Hamilton

Research output: Contribution to journalArticle

Abstract

Protein surface recognition is largely unexplored owing to the large solvent exposed surface and lack of proper molecular scaffolds to match the binding residues. This review describes the design, synthesis, and fluorescence binding studies of functionalized porphyrins aimed at targeting surface residues of proteins through complementary recognition. The pattern of lysine residues surrounding the heme-edge of horse heart cytochrome c has been targeted by tetraphenylporphyrin and tetrabiphenylporphyrin receptors that bind with nano- and sub-nanomolar affinity. Other designed porphyrin-based receptors also recognize potassium channel as a target. The strategies for protein surface recognition offer a new use for porphyrins as molecular scaffolds.

Original languageEnglish (US)
Pages (from-to)141-147
Number of pages7
JournalJournal of Porphyrins and Phthalocyanines
Volume8
Issue number1-3
StatePublished - 2004

Fingerprint

Porphyrins
Membrane Proteins
Scaffolds
Potassium Channels
Cytochromes c
Heme
Lysine
Fluorescence
Proteins

Keywords

  • Fluorescence studies
  • Porphyrins
  • Protein surface recognition
  • Protein-protein interactions

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Protein surface recognition by porphyrin-based receptors. / Tsou, Lun K.; Jain, Rishi K.; Hamilton, Andrew.

In: Journal of Porphyrins and Phthalocyanines, Vol. 8, No. 1-3, 2004, p. 141-147.

Research output: Contribution to journalArticle

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