O2-binding properties of albumin hybrid incorporating porphyrinatoiron having histidine derivative

Akito Nakagawa; Teruyuki Komatsu; Eishun Tsuchida; Makoto Iiduka; Shinji Takeoka

O₂-binding properties of albumin hybrid incorporating porphyrinatoiron having histidine derivative

Akito Nakagawa^*, Teruyuki Komatsu, Eishun Tsuchida, Makoto Iiduka, Shinji Takeoka

^*Corresponding author for this work

School of Advanced Science and Engineering

Research output: Contribution to conference › Paper › peer-review

Abstract

We have evaluated the dioxygen binding properties of albumin hybrid incorporating porphyrinatoirons having histidine derivative [FeP(His), FeP(MHis)]. They were synthesized via 9 steps from 5,10,15,20-tetrakis(o- aminophenyl)porphyrin. FeP(His) binds histidine and FeP(MHis) binds 1-methylhistidine as a proximal base. Both hemes could be incorporated into human serum albumin (HSA) providing HSA hybrid [HSA-FeP(His) or HSA-FeP(MHis)] in the buffer solution (pH 7.3). HSA-FeP(MHis) showed a low O ₂-binding affinity (P₅₀: 15 Torr) and a high O ₂-dissociation rate constant in comparison to HSA-FeP(His). This is due to the steric hindrance for the coordination of the proximal base derived from the methylene group at 4-posititon of imidazole ring in FeP(MHis). HSA-FeP(MHis) can be utilized as a new artificial O₂-therapeutics.

Original language	English
Number of pages	1
Publication status	Published - 2006 Dec 1
Event	55th Society of Polymer Science Japan Symposium on Macromolecules - Toyama, Japan Duration: 2006 Sept 20 → 2006 Sept 22

Other

Other	55th Society of Polymer Science Japan Symposium on Macromolecules
Country/Territory	Japan
City	Toyama
Period	06/9/20 → 06/9/22

Keywords

Albumin
Artificial blood
Heme
Hemoprotein
Porphyrin

ASJC Scopus subject areas

Engineering(all)

Cite this

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title = "O2-binding properties of albumin hybrid incorporating porphyrinatoiron having histidine derivative",

abstract = "We have evaluated the dioxygen binding properties of albumin hybrid incorporating porphyrinatoirons having histidine derivative [FeP(His), FeP(MHis)]. They were synthesized via 9 steps from 5,10,15,20-tetrakis(o- aminophenyl)porphyrin. FeP(His) binds histidine and FeP(MHis) binds 1-methylhistidine as a proximal base. Both hemes could be incorporated into human serum albumin (HSA) providing HSA hybrid [HSA-FeP(His) or HSA-FeP(MHis)] in the buffer solution (pH 7.3). HSA-FeP(MHis) showed a low O 2-binding affinity (P50: 15 Torr) and a high O 2-dissociation rate constant in comparison to HSA-FeP(His). This is due to the steric hindrance for the coordination of the proximal base derived from the methylene group at 4-posititon of imidazole ring in FeP(MHis). HSA-FeP(MHis) can be utilized as a new artificial O2-therapeutics.",

keywords = "Albumin, Artificial blood, Heme, Hemoprotein, Porphyrin",

author = "Akito Nakagawa and Teruyuki Komatsu and Eishun Tsuchida and Makoto Iiduka and Shinji Takeoka",

year = "2006",

month = dec,

day = "1",

language = "English",

note = "55th Society of Polymer Science Japan Symposium on Macromolecules ; Conference date: 20-09-2006 Through 22-09-2006",

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TY - CONF

T1 - O2-binding properties of albumin hybrid incorporating porphyrinatoiron having histidine derivative

AU - Nakagawa, Akito

AU - Komatsu, Teruyuki

AU - Tsuchida, Eishun

AU - Iiduka, Makoto

AU - Takeoka, Shinji

PY - 2006/12/1

Y1 - 2006/12/1

N2 - We have evaluated the dioxygen binding properties of albumin hybrid incorporating porphyrinatoirons having histidine derivative [FeP(His), FeP(MHis)]. They were synthesized via 9 steps from 5,10,15,20-tetrakis(o- aminophenyl)porphyrin. FeP(His) binds histidine and FeP(MHis) binds 1-methylhistidine as a proximal base. Both hemes could be incorporated into human serum albumin (HSA) providing HSA hybrid [HSA-FeP(His) or HSA-FeP(MHis)] in the buffer solution (pH 7.3). HSA-FeP(MHis) showed a low O 2-binding affinity (P50: 15 Torr) and a high O 2-dissociation rate constant in comparison to HSA-FeP(His). This is due to the steric hindrance for the coordination of the proximal base derived from the methylene group at 4-posititon of imidazole ring in FeP(MHis). HSA-FeP(MHis) can be utilized as a new artificial O2-therapeutics.

AB - We have evaluated the dioxygen binding properties of albumin hybrid incorporating porphyrinatoirons having histidine derivative [FeP(His), FeP(MHis)]. They were synthesized via 9 steps from 5,10,15,20-tetrakis(o- aminophenyl)porphyrin. FeP(His) binds histidine and FeP(MHis) binds 1-methylhistidine as a proximal base. Both hemes could be incorporated into human serum albumin (HSA) providing HSA hybrid [HSA-FeP(His) or HSA-FeP(MHis)] in the buffer solution (pH 7.3). HSA-FeP(MHis) showed a low O 2-binding affinity (P50: 15 Torr) and a high O 2-dissociation rate constant in comparison to HSA-FeP(His). This is due to the steric hindrance for the coordination of the proximal base derived from the methylene group at 4-posititon of imidazole ring in FeP(MHis). HSA-FeP(MHis) can be utilized as a new artificial O2-therapeutics.

KW - Albumin

KW - Artificial blood

KW - Heme

KW - Hemoprotein

KW - Porphyrin

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AN - SCOPUS:33846134421

T2 - 55th Society of Polymer Science Japan Symposium on Macromolecules

Y2 - 20 September 2006 through 22 September 2006

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