Interaction between chlorpromazine and human serum albumin

Masami Tanaka, Seizo Masuda, Keiji Minagawa, Takeshi Mori

Research output: Chapter in Book/Report/Conference proceedingConference contribution


The interaction between Chlorpromazine (CPM) and human serum albumin (HSA) was investigated by equilibrium dialysis. Since the binding constant of CPM to HSA was independent of ionic strength and decreased with increase of alkyl chain length of fatty acid added, the interaction between CPM and HSA was considered to be due to hydrophobic mechanism. Chemical shifts in 1H-NMR spectra of CPM were independent of the concentration of CPM and addition of HSA. Spin-lattice relaxation time (T1) and spin-spin relaxation time (T2) of respective protons of CPM were independent of the concentration, but depended on the concentration of HSA added. The binding position of CPM to HSA was considered to involve the hydrophobic aromatic moiety of CPM from the ratio of spin-spin relaxation rates (1/T2) of CPM bound to HSA and free CPM.

Original languageEnglish
Title of host publicationPolymer Preprints, Japan - 55th SPSJ Annual Meeting
Number of pages1
Publication statusPublished - 2006
Externally publishedYes
Event55th SPSJ Annual Meeting - Nagoya, Japan
Duration: May 24 2006May 26 2006


Other55th SPSJ Annual Meeting

All Science Journal Classification (ASJC) codes

  • Engineering(all)


Dive into the research topics of 'Interaction between chlorpromazine and human serum albumin'. Together they form a unique fingerprint.

Cite this