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Albumin aggregation promoted by protoporphyrin in vitro

Natalya Shamil'evna Lebedeva 1
Natalya Shamil'evna Lebedeva
, 
Elena Sergeevna Yurina 1
Elena Sergeevna Yurina
, 
Yury Aleksandrovich Gubarev 1
Yury Aleksandrovich Gubarev
, 
Aleksey N Kiselev 1
Aleksey N Kiselev
, 
Sergei Aleksandrovich Syrbu 1
Sergei Aleksandrovich Syrbu
10.1016/j.mencom.2020.03.027
Published 2020-03-02
Communication , Volume 30, Issue 2, 211-213
7
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Lebedeva N. S. et al. Albumin aggregation promoted by protoporphyrin in vitro // Mendeleev Communications. 2020. Vol. 30. No. 2. pp. 211-213.
GOST all authors (up to 50) Copy
Lebedeva N. S., Yurina E. S., Gubarev Y. A., Kiselev A. N., Syrbu S. A. Albumin aggregation promoted by protoporphyrin in vitro // Mendeleev Communications. 2020. Vol. 30. No. 2. pp. 211-213.
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TY - JOUR
DO - 10.1016/j.mencom.2020.03.027
UR - https://mendcomm.colab.ws/publications/10.1016/j.mencom.2020.03.027
TI - Albumin aggregation promoted by protoporphyrin in vitro
T2 - Mendeleev Communications
AU - Lebedeva, Natalya Shamil'evna
AU - Yurina, Elena Sergeevna
AU - Gubarev, Yury Aleksandrovich
AU - Kiselev, Aleksey N
AU - Syrbu, Sergei Aleksandrovich
PY - 2020
DA - 2020/03/02
PB - Mendeleev Communications
SP - 211-213
IS - 2
VL - 30
ER -
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@article{2020_Lebedeva,
author = {Natalya Shamil'evna Lebedeva and Elena Sergeevna Yurina and Yury Aleksandrovich Gubarev and Aleksey N Kiselev and Sergei Aleksandrovich Syrbu},
title = {Albumin aggregation promoted by protoporphyrin in vitro},
journal = {Mendeleev Communications},
year = {2020},
volume = {30},
publisher = {Mendeleev Communications},
month = {Mar},
url = {https://mendcomm.colab.ws/publications/10.1016/j.mencom.2020.03.027},
number = {2},
pages = {211--213},
doi = {10.1016/j.mencom.2020.03.027}
}
MLA
Cite this
MLA Copy
Lebedeva, Natalya Shamil'evna, et al. “Albumin aggregation promoted by protoporphyrin in vitro.” Mendeleev Communications, vol. 30, no. 2, Mar. 2020, pp. 211-213. https://mendcomm.colab.ws/publications/10.1016/j.mencom.2020.03.027.

Keywords

aggregation
albumin
fluorescence
IR spectroscopy
porphyrin
UV-VIS spectroscopy

Abstract

Protoporphyrin upon its binding with serum albumin changes its secondary structure due to the conversion of part of α helices into β-folding. This process results in the association of albumin globules in vitro.

References

1.
Interactions of hemin with bovine serum albumin and human hemoglobin: A fluorescence quenching study.
Makarska-Bialokoz M.
Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy, 2018
2.
Chiabrando D., Mercurio S., Tolosano E.
Haematologica, 2014
3.
Heme metabolism and erythropoiesis
Chung J., Chen C., Paw B.H.
Current Opinion in Hematology, 2012
4.
The porphyrias: advances in diagnosis and treatment
Balwani M., Desnick R.J.
Hematology / the Education Program of the American Society of Hematology. American Society of Hematology. Education Program, 2012
5.
10.1016/j.mencom.2020.03.027_bib0025
Miller
Biochem. Mol. Biol. Int., 1994
7.
Hemin-induced lipid membrane disorder and increased permeability: a molecular model for the mechanism of cell lysis.
Schmitt T.H., Frezzatti W.A., Schreier S.
Archives of Biochemistry and Biophysics, 1993
8.
Pro-oxidant and cytotoxic effects of circulating heme
Jeney V., Balla J., Yachie A., Varga Z., Vercellotti G.M., Eaton J.W., Balla G.
Blood, 2002
9.
The role of transporters in cellular heme and porphyrin homeostasis
KRISHNAMURTHY P., XIE T., SCHUETZ J.
Pharmacology and Therapeutics, 2007
10.
Comparison of the complexing ability of zinc (II) porphyrins to diamines
Lebedeva N.S., Yurina E.S., Gubarev Y.A., Syrbu S.A.
Journal of Molecular Liquids, 2019
12.
Lebedeva N.S., Yurina E.S., Gubarev Y.A., Syrbu S.A., Pechnikova N.L.
Mendeleev Communications, 2018
13.
10.1016/j.mencom.2020.03.027_bib0065
Siddiqi
Front. Biosci., Elite Ed., 2017
15.
Greatly enhanced binding of a cationic porphyrin towards bovine serum albumin by cucurbit[8]uril
Lei W., Jiang G., Zhou Q., Zhang B., Wang X.
Physical Chemistry Chemical Physics, 2010
16.
Site-Selective Binding and Dual Mode Recognition of Serum Albumin by a Squaraine Dye
Jisha V.S., Arun K.T., Hariharan M., Ramaiah D.
Journal of the American Chemical Society, 2006
17.
Activatable albumin-photosensitizer nanoassemblies for triple-modal imaging and thermal-modulated photodynamic therapy of cancer
Hu D., Sheng Z., Gao G., Siu F., Liu C., Wan Q., Gong P., Zheng H., Ma Y., Cai L.
Biomaterials, 2016
18.
Human serum albumin: from bench to bedside.
Fanali G., di Masi A., Trezza V., Marino M., Fasano M., Ascenzi P.
Molecular Aspects of Medicine, 2012
19.
Crystal structural analysis of human serum albumin complexed with hemin and fatty acid
Zunszain P.A., Ghuman J., Komatsu T., Tsuchida E., Curry S.
BMC Structural Biology, 2003
20.
The Atomic Structure of Human Methemalbumin at 1.9 Å
Wardell M., Wang Z., Ho J.X., Robert J., Ruker F., Ruble J., Carter D.C.
Biochemical and Biophysical Research Communications, 2002
23.
Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin
Hu Y., Liu Y., Wang J., Xiao X., Qu S.
Journal of Pharmaceutical and Biomedical Analysis, 2004
24.
The Use and Misuse of FTIR Spectroscopy in the Determination of Protein Structure
Jackson M., Mantsch H.H.
Critical Reviews in Biochemistry and Molecular Biology, 1995
25.
10.1016/j.mencom.2020.03.027_bib0125
Cooper
Physical Methods to Characterize Pharmaceutical Proteins (Pharmaceutical Biotechnology, vol. 7), 1995
27.
The Infared Spectra of Metalloporphyrins (4000-160 Cm-1)
Boucher L.J., Katz J.J.
Journal of the American Chemical Society, 1967