Recognition and Fluorescence Sensing of Specific Amino Acid Residue on Protein Surface Using Designed Molecules

Akio Ojida, Yoshifumi Miyahara, Takahiro Kohira, Itaru Hamachi

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Many biological processes are mediated by surface recognition between proteins. Small molecules that recognize and bind a specific region of a protein surface may be promising agents for disrupting certain protein-protein surface interactions, which consequently leads to regulation of cellar functions. This article describes our recent efforts toward the development of the designed small molecules, which can recognize histidine or phosphorylated amino acid residues on peptide surfaces in a sequence-selective manner. These results demonstrate that cooperative metal-ligand interaction is powerful for tight and selective binding to the specific amino acid residues of proteins in aqueous medium.

Original languageEnglish
Pages (from-to)177-184
Number of pages8
JournalBiopolymers - Peptide Science Section
Volume76
Issue number2
DOIs
Publication statusPublished - May 6 2004

Fingerprint

Amino acids
Membrane Proteins
Fluorescence
Proteins
Amino Acids
Molecules
Biological Phenomena
Histidine
Metals
Ligands
Peptides

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry

Cite this

Recognition and Fluorescence Sensing of Specific Amino Acid Residue on Protein Surface Using Designed Molecules. / Ojida, Akio; Miyahara, Yoshifumi; Kohira, Takahiro; Hamachi, Itaru.

In: Biopolymers - Peptide Science Section, Vol. 76, No. 2, 06.05.2004, p. 177-184.

Research output: Contribution to journalArticle

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