4th EucheMs chemistry congress

Poster Session 1
s888
chem. Listy 106, s587–s1425 (2012)
Poster session 1 - life sciences
7. Matile, S.; Sakai, N. In Analytical Methods in
Supramolecular Chemistry; Wiley-VCH Verlag GmbH &
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10. Guo, D. S.; Uzunova, V. D.; Su, X.; Liu, Y.; Nau, W. M.
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Keywords: peptides; liposomes; membrane proteins;
fluorescence; fluorescent dyes; supramolecular chemistry;
macrocycles; lipids;
4 th EucheMs chemistry congress
P - 0 0 5 7
uSe of A non-heMe iron PeroxidASe in
heMoGLoBin And heMerythrin-BASed BLood
SuBStituteS
G. d. hAthAzi 1 , A. C. Mot 1 , f. deAC 1 , i. LuPAn 2 ,
e. fiSher-fodor 3 , G. dAMiAn 4 , d. M. Kurtz Jr 5 ,
r. SiLAGhi duMitreSCu 1
1 Babes-Bolyai University, Faculty of Chemistry and Chemical
Engineering, Cluj-Napoca, Romania
2 Babes-Bolyai University, Faculty of Biology and Geology,
Cluj-Napoca, Romania
3 Ion Chiricuta Cancer Institute, Comprehensive Cancer Center,
Cluj-Napoca, Romania
4 Babes-Bolyai University, Department of Physics, Cluj-Napoca,
Romania
5 University of Texas at San Antonio, One UTSA Circle, San
Antonio, USA
Hemoglobin-based potential artificial oxygen carriers have
been described and examined extensively.However, their
applicability so far has been limited due to known in vivo toxicity
issues. As many of these issues can be linked to oxidative stress,
strategies were proposed for limiting this toxicity by adding
antioxidant small molecules or enzymes to chemically-derivatized
or encapsulated hemoglobin. Hemerythrin has distinctly smaller
reactivity than hemoglobin towards oxidative and nitrosative
stress agents, and also shows a remarkably smaller tendency to
generate toxic free radicals in such reactions.
The non-heme iron peroxidase, rubrerythrin (Rbr), shows as
an interesting feature the ability to reduce hydrogen peroxide
without involving strongly-oxidizing and free-radical-creating
powerful oxidants such as Compounds I and II (formally Fe(IV)
in contrast with heme-containing peroxidases and catalases.
Morevoer, the K for hydrogen peroxide is two orders of
m
magnitude lower in Rbr compared to peroxidases and catalases.
Therefore, it may be used as a useful ingredient in protein-based
artificial oxygen carriers. Hemoglobin (Hb) and hemerythrin (Hr),
can each be co-polymerized with rubrerythrin using
gluteraldehyde as cross-linking agent. These co-polymers show
additional peroxidase activity compared to Hb-only and Hr-only
polymers, respectively. Reported here are protocols for chemical
crosslinking of hemerythrin and hemoglobin with small amounts
of rubrerythrin, leading to products with increased capability for
removing hydrogen peroxide, offering promise as less toxic
artificial oxygen carriers/blood substitutes.
Tests on human umbilical vein endothelial cells (HUVEC)
reveal slightly better performance of the Rbr co-polymers
compared to controls, as measured at 24 hours but not at later
times.
Acknowledgements: the work shown here has been supported
by the Romanian Ministry for Education and Research (grant
PCCE 140/2008) and by PhD scholarships to ACM and FD
(Contract POSDRU/88/1.5/S/60185 – “Innovative doctoral
studies in a knowledge based society”).
Keywords: blood substitutes; Rubrerythrin; co-polymers;
hemoglobin; hemerythrin;
AUGUst 26–30, 2012, PrAGUE, cZEcH rEPUbLIc