Interaction between bumetanide and human serum albumin

Masami Tanaka; Seizo Masuda; Keiji Minagawa; Takeshi Mori

Interaction between bumetanide and human serum albumin

Masami Tanaka, Seizo Masuda, Keiji Minagawa, Takeshi Mori

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution

Abstract

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

Original language	English
Title of host publication	54th SPSJ Annual Meeting 2005 - Polymer Preprints, Japan
Pages	2063
Number of pages	1
Volume	54
Edition	1
Publication status	Published - 2005
Externally published	Yes
Event	54th SPSJ Annual Meeting 2005 - Yokohama, Japan Duration: May 25 2005 → May 27 2005

Other

Other	54th SPSJ Annual Meeting 2005
Country/Territory	Japan
City	Yokohama
Period	5/25/05 → 5/27/05

All Science Journal Classification (ASJC) codes

Engineering(all)

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title = "Interaction between bumetanide and human serum albumin",

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

author = "Masami Tanaka and Seizo Masuda and Keiji Minagawa and Takeshi Mori",

year = "2005",

language = "English",

volume = "54",

pages = "2063",

booktitle = "54th SPSJ Annual Meeting 2005 - Polymer Preprints, Japan",

edition = "1",

note = "54th SPSJ Annual Meeting 2005 ; Conference date: 25-05-2005 Through 27-05-2005",

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TY - GEN

T1 - Interaction between bumetanide and human serum albumin

AU - Tanaka, Masami

AU - Masuda, Seizo

AU - Minagawa, Keiji

AU - Mori, Takeshi

PY - 2005

Y1 - 2005

N2 - The interaction between Bumetanide (BMD) and human serum albumin (HSA) was investigated by equilibrium dialysis. Since the binding constant of BMD to HSA was independent of ionic strength and decreased with increase of alkyl chain length of fatty acid added, the interaction between BMD and HSA was considered to be due to hydrophobic mechanism. Chemical shifts in 1H-NMR spectra of BMD were independent of the concentration of BMD and addition of HSA. Spin-lattice relaxation time (T1) and spin-spin relaxation time (T2) of respective protons of BMD were independent of the concentration, but depended on the concentration of HSA added. The binding position of BMD to HSA was considered to involve the hydrophobic aromatic moiety of BMD from the ratio of spin-spin relaxation rates (1/T2) of BMD bound to HSA and free BMD.

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

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M3 - Conference contribution

AN - SCOPUS:33645650603

VL - 54

SP - 2063

BT - 54th SPSJ Annual Meeting 2005 - Polymer Preprints, Japan

T2 - 54th SPSJ Annual Meeting 2005

Y2 - 25 May 2005 through 27 May 2005

ER -

Interaction between bumetanide and human serum albumin

Abstract

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All Science Journal Classification (ASJC) codes

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