Affordable Access

Comparative study of the binding of pepsin to four alkaloids by spectrofluorimetry

Authors
Publisher
Elsevier B.V.
Volume
108
Identifiers
DOI: 10.1016/j.saa.2013.01.077
Keywords
  • Pepsin
  • Caffeine
  • Aminophylline
  • Acefylline
  • Diprophylline
  • Interaction
Disciplines
  • Biology
  • Physics

Abstract

Abstract The interactions between pepsin and four alkaloids, including caffeine (Caf), aminophylline (Ami), acefylline (Ace), diprophylline (Dip), were investigated by fluorescence, UV–visible absorption, resonance light scattering, synchronous fluorescence spectroscopy and 3D spectroscopy under mimic physiological conditions. The results revealed that Caf (Ami/Ace/Dip) caused the fluorescence quenching of pepsin by the formation of Caf (Ami/Ace/Dip)-pepsin complex. The binding constants and thermodynamic parameters at three different temperatures, the binding locality and the binding power were obtained. The hydrophobic and electrostatic interactions were the predominant intermolecular forces to stabilize the complex. Results showed that aminophylline was the stronger quencher and bound to pepsin with higher affinity than other three alkaloids.

There are no comments yet on this publication. Be the first to share your thoughts.