XAFS studies of the synthetic substitutes of hemozoin
Source abstract
Abstract
The local atomic structure around iron atoms of two synthetic analogues of malarial pigment product is characterized by iron K-edge X-ray absorption fine structure spectroscopy (XAFS). Malarial pigment, also termed hemozoin, is a condensed phase of ferriprotoporphyrin-IX dimers, and is structurally identical to the synthetic material hematin anhydride, which is also termed IS-hematin. Synthetic hemozoin analogues might serve as surrogates or models of malaria pigment for a range of fundamental laboratory methods, for example the design of new antimalarials. Two new iron(III)(protoporphyrin-IX) analogues, based on meso- and deuteroporphyrin are considered. Both new condensed phases are slightly soluble in many organic solvents. In the present work, the detailed examination of X-ray absorption spectra of monomer- and dimer-ferriprotoporphyrin-IX-based compounds is discussed. Parameters obtained by quantitative spectra analysis allow us to classify the new synthetic equivalents of the parasite product as dimer materials. X-ray absorption technique was able to distinguish dimer from monomer structures based on the structural disorder parameters of oxygen ligand bonding. (C) 2010 Elsevier B.V. All rights reserved.
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Research context
OpenAlex topics: Porphyrin and Phthalocyanine Chemistry · Photodynamic Therapy Research Studies · Malaria Research and Control
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (15)
Show source-provided references
1. G. M. Luncisi. De Noxiis Paludum Effluvius Eorumque Remediis. Rome: J.M. Salvioni (1717).10.5962/bhl.title.50605 ↗
2. Fitch · J. Biol. Chem. · 1987 · 262 · 1555210.1016/S0021-9258(18)47761-7 ↗
3. Slater · Proc. Natl Acad. Sci. USA · 1991 · 88 · 32510.1073/pnas.88.2.325 ↗
4. Bohle · J. Biol. Chem. · 1997 · 272 · 71310.1074/jbc.272.2.713 ↗
5. Pagola · Nature · 2000 · 404 · 30710.1038/35005132 ↗
6. Walczak · Nucl. Instrum. Meth. Phys. Res. B · 2005 · 238 · 3210.1016/j.nimb.2005.06.014 ↗
7. Bohle · Acta Cryst. · 2002 · 58 · 1752
8. K. V. Klementiev, VIPER for Windows, freeware; K.V.Klementev, J. Phys. D: Appl. Phys. 34 (2001) 209–217.10.1088/0022-3727/34/2/309 ↗
9. Binsted · Biochemistry · 1992 · 31 · 1211710.1021/bi00163a021 ↗
10. Gurman · J. Phys. C · 1984 · 17 · 14310.1088/0022-3719/17/1/019 ↗
11. Gurman · J. Phys. C · 1986 · 19 · 184510.1088/0022-3719/19/11/021 ↗
12. Gurman · J. Phys. C · 1988 · 21 · 369910.1088/0022-3719/21/19/020 ↗
13. Boffi · Biophys. J. · 1999 · 77 · 114310.1016/S0006-3495(99)76965-1 ↗
14. Della Longa · Biochim. Biophys. Acta · 1996 · 1294 · 7210.1016/0167-4838(95)00270-7 ↗
15. Sienkiewicz · J. Am. Chem. Soc. · 2006 · 128 · 453410.1021/ja058420h ↗