Energy transfer from tryptophan residues of proteins to 8-anilinonaphthalene-1-sulfonate

Long sen Chang, Ehr ya Wen, Jan-Jong Hung, Chung chang Chang

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)

Abstract

The binding of the apolar fluorescent dye 8-anilinonaphthalene-1-sulfonate (ANS) to bovine serum albumin (BSA), phospholipase A2 (PLA2), ovalbumin, lysozyme, cobrotoxin and N-acetyltryptophanamide was used to assess the factors affecting the efficiency of energy transfer from Trp residues to the ANS molecule. We found that the efficiency of energy transfer from Trp residues to ANS was associated with the ability of proteins to enhance the ANS fluorescence. At the same molar concentration of protein, BSA enhanced ANS fluorescence most among these proteins; its Trp fluorescence was drastically quenched by the addition of ANS. Fluorescence enhancement of ANS in PLA2-ANS complex increased upon addition of Ca2+ or change of the buffer to acidic pH, resulting in a higher efficiency of energy transfer from Trp residues to ANS. There was limited ANS fluorescence enhancement with ovalbumin, lysozyme, cobrotoxin, and N-acetyltryptophanamide and a less efficient quenching in Trp fluorescence. The capabilities of proteins for binding with ANS correlated with the decrease in their Trp fluorescence being quenching by ANS. However, the microenvironment surrounding Trp residues of proteins did not affect the energy transfer. Based on these results, the factors that affected the energy transfer from Trp residues to ANS are discussed.

Original languageEnglish
Pages (from-to)635-640
Number of pages6
JournalJournal of Protein Chemistry
Volume13
Issue number7
DOIs
Publication statusPublished - 1994 Oct 1

All Science Journal Classification (ASJC) codes

  • Biochemistry

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