Probing the Structural Requirements for the Binding of Aurones to ATP

Abstract

Aurones, found in flowers and fruits, contribute to their golden-yellow pigmentation. Their activities involve interactions with ATP-binding domains. Aurone frameworks are prepared by condensation of benzofuranones with aldehydes. This study explores the importance of hydrogen bond-accepting and donating groups in aurone molecules. Aurones exhibit photophysical properties, including absorption and emission spectra in various solvents with different polarity and protic characteristics. The peak absorption intensity reflects the wavelength at which aurones absorb the most energy, crucial for understanding light emission. The maximum emission ranges correspond to the wavelength at which aurones absorb light most effectively, providing insights into their photophysical behavior in different environments. An optimal excitation wavelength indicates the strongest interaction with light, suitable for investigating aurone fluctuations during peak activity and exploring the YME1L AAA+ protein, which exhibits properties like protein kinases. Aurone showing significant differences in fluorescence when mixed with the YME1L AAA+ protein compared to isolation, demonstrate aurone interactions with the protein domain. After determining the optimal excitation wavelength, experiments compared the presence and absence of protein in aurone solutions. Aurones showing distinct signals in solutions containing only aurone versus both aurone and protein, indicate their binding capability, while aurones with minimal differences suggested poor protein binding models and were excluded. These signals supported protein binding and prompted further investigation at YME1L AAA+ protein contacts. Aurones exhibiting decreased fluorescence intensity with increasing YMEIL AAA+ protein concentrations suggest potential binding interactions. Concentration also influenced tryptophan fluorescence, but inaccurate results were obtained due to an incorrect cuvette.