scholarly journals The protective effect of lactoferrin on ventral mesencephalon neurons against MPP+ is not connected with its iron binding ability

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Jun Wang ◽  
Mingxia Bi ◽  
Huiying Liu ◽  
Ning Song ◽  
Junxia Xie
Keyword(s):  
Protective Effect ◽  
Iron Binding ◽  
Ventral Mesencephalon ◽  
Binding Ability

scholarly journals A Novel Star Like Eight-Arm Polyethylene Glycol-Deferoxamine Conjugate for Iron Overload Therapy

Pharmaceutics ◽  
2020 ◽  
Vol 12 (4) ◽  
pp. 329
Author(s):  
Bohong Yu ◽  
Yinxian Yang ◽  
Qi Liu ◽  
Aiyan Zhan ◽  
Yang Yang ◽  
...  
Keyword(s):  
Polyethylene Glycol ◽  
Iron Overload ◽  
Iron Chelator ◽  
Iron Chelators ◽  
Iron Binding ◽  
Binding Ability ◽  
Amide Bonds ◽  
Plasma Half Life ◽  
Iron Chelator Deferoxamine

The traditional iron chelator deferoxamine (DFO) has been widely used in the treatment of iron overload disease. However, DFO has congenital disadvantages, including a very short circular time and non-negligible toxicity. Herein, we designed a novel multi-arm conjugate for prolonging DFO duration in vivo and reducing cytotoxicity. The star-like 8-arm-polyethylene glycol (8-arm-PEG) was used as the macromolecular scaffold, and DFO molecules were bound to the terminals of the PEG branches via amide bonds. The conjugates displayed comparable iron binding ability to the free DFO. Furthermore, these macromolecule conjugates could significantly reduce the cytotoxicity of the free DFO, and showed satisfactory iron clearance capability in the iron overloaded macrophage RAW 246.7. The plasma half-life of the 8-arm-PEG-DFO conjugate was about 190 times than that of DFO when applied to an intravenously administered rat model. In conclusion, research indicated that these star-like PEG-based conjugates could be promising candidates as long circulating, less toxic iron chelators.

scholarly journals Serological and fluorescence studies of the heat stability of bovine lactoferrin

1979 ◽  
Vol 46 (1) ◽  
pp. 83-93 ◽  
Author(s):  
Augustin Baer ◽  
Marko Oroz ◽  
Bernard Blanc
Keyword(s):  
Metal Binding ◽  
Binding Sites ◽  
Complement Fixation ◽  
Heat Stability ◽  
Heat Denaturation ◽  
Bovine Lactoferrin ◽  
Iron Binding ◽  
Binding Ability ◽  
Fluorescence Studies ◽  
Tryptophan Residues

SUMMARYThe heat denaturation of Fe-saturated lactoferrin (If) and Fe-free lactoferrin (apo-lf) was studied using the methods of micro-complement fixation and fluorescence. It was established that the change in conformation of apo-lf, induced by iron binding, conferred a higher heat stability to the molecule: the changes were observed at temperatures above 40 °C for apo-lf and above 60 °C for If. The Fe-binding ability of the protein was partially independent of the degree of denaturation. Fluorescence analyses indicated that tryptophan residues were probably not directly involved in the metal binding. There was no evidence of antibodies interfering with the binding sites.

Comparison of Iron-Binding Ability Between Thr70-NapA and Ser70-NapA ofHelicobacter pylori

Helicobacter ◽  
2015 ◽  
Vol 21 (3) ◽  
pp. 192-200 ◽  
Author(s):  
Weiran Shan ◽  
Hsiang-fu Kung ◽  
Ruiguang Ge
Keyword(s):  
Iron Binding ◽  
Binding Ability

scholarly journals Enzymatic Hydrolysis of Heated Whey: Iron-Binding Ability of Peptides and Antigenic Protein Fractions

2007 ◽  
Vol 90 (9) ◽  
pp. 4033-4042 ◽  
Author(s):  
S.B. Kim ◽  
I.S. Seo ◽  
M.A. Khan ◽  
K.S. Ki ◽  
W.S. Lee ◽  
...  
Keyword(s):  
Enzymatic Hydrolysis ◽  
Protein Fractions ◽  
Iron Binding ◽  
Binding Ability ◽  
Antigenic Protein ◽  
Hydrolysis Of

scholarly journals Lactoferrin: a review

2008 ◽  
Vol 53 (No. 9) ◽  
pp. 457-468 ◽  
Author(s):  
L. Adlerova ◽  
A. Bartoskova ◽  
M. Faldyna
Keyword(s):  
Biological Properties ◽  
Exocrine Glands ◽  
Iron Binding ◽  
Biological Functions ◽  
Binding Ability ◽  
Antiparasitic Activity ◽  
Cell Proliferation And Differentiation ◽  
Proliferation And Differentiation ◽  
Specific Granules ◽  
The Relationship

This review discusses the biological properties of the glycoprotein lactoferrin. Lactoferrin has been identified in secretions from exocrine glands and in specific granules of neutrophils. After degranulation, neutrophils become the main source of lactoferrin in blood plasma. Lactoferrin possesses various biological functions, including roles in iron metabolism, cell proliferation and differentiation, and antibacterial, antiviral, and antiparasitic activity. Many of these functions do not appear to be connected with its iron binding ability. Of late, lactoferrin concentrations have been measured mostly in humans but also in some other species. However, the relationship between its concentration and physiological or pathological effects on body functions is not yet well characterised.

scholarly journals ДІАГНОСТИЧНА ЦІННІСТЬ ДОСЛІДЖЕННЯ ТРАНСФЕРИНУ НА РІЗНИХ СТАДІЯХ РОЗВИТКУ АНЕМІЇ ЗЛОЯКІСНОГО НОВОУТВОРЕННЯ У ПАЦІЄНТІВ ІЗ УРОТЕЛІАЛЬНИМ РАКОМ СЕЧОВОГО МІХУРА

World Science ◽  
2019 ◽  
Vol 1 (12(52)) ◽  
pp. 25-31
Author(s):  
Станіслав Видиборець ◽  
Дмитро Борисенко
Keyword(s):  
Iron Deficiency ◽  
Urinary Bladder ◽  
Urothelial Cancer ◽  
Physiological Role ◽  
Clinical Importance ◽  
Laboratory Diagnostics ◽  
Iron Binding ◽  
Malignant Growth ◽  
Binding Ability ◽  
The Given

In clause the items of information on transport protein of iron - transferrin are stated. Its physiological role and clinical importance is shown.The content of iron in the blood whey (SZH) and index of general iron- binding ability of the whey (OZHSS) were determined by batofenantrolin method. The index of the unsaturated iron-binding ability of the whey (NZHSS) was calculated as a difference between OZHSS and SZH. The coefficient of saturation of transferrin by iron (KNTZH) was determined as correlation of maintenance of SZH to OZHSS. The contents of transferrin (TF) was determined on the index of OZHSS, ferritin (FN) by a radiometric method. Dynamics of the contents of the transferrin of the patients with anemia of malignant growth in patients with urothelial cancer of the urinary bladder. The conclusion about importance of the given parameter for laboratory diagnostics of iron deficiency condition and anemia of malignant growth is made.

scholarly journals Caffeic Acid Phenyl Ester (CAPE) Protects against Iron-Mediated Cellular DNA Damage through Its Strong Iron-Binding Ability and High Lipophilicity

Antioxidants ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 798
Author(s):  
Bo Shao ◽  
Li Mao ◽  
Miao Tang ◽  
Zhu-Ying Yan ◽  
Jie Shao ◽  
...  
Keyword(s):  
Dna Damage ◽  
Caffeic Acid ◽  
Caffeic Acid Phenethyl Ester ◽  
Coordination Mechanism ◽  
Iron Binding ◽  
Binding Ability ◽  
Ethyl Ferulate ◽  
Labile Iron Pool ◽  
Treatment And Prevention ◽  
Cellular Dna

Caffeic acid phenethyl ester (CAPE) and its structurally-related caffeic acid (CA), ferulic acid (FA) and ethyl ferulate (EF) are constituents of honeybee propolis that have important pharmacological activities. This study found that CAPE—but not CA, FA, and EF—could effectively prevent cellular DNA damage induced by overloaded iron through decreasing the labile iron pool (LIP) levels in HeLa cells. Interestingly, CAPE was found to be more effective than CA in protecting against plasmid DNA damage induced by Fe(II)–H2O2 or Fe(III)–citrate–ascorbate-H2O2 via the inhibition of hydroxyl radical (•OH) production. We further provided more direct and unequivocal experimental evidences for the formation of inactive CAPE/CA–iron complexes. CAPE was found to have a stronger iron-binding ability and a much higher lipophilicity than CA. Taken together, we propose that the esterification of the carboxylic moiety with phenethyl significantly enhanced the iron-binding ability and lipophilicity of CAPE, which is also responsible for its potent protection against iron-mediated cellular DNA damage. A study on the iron coordination mechanism of such natural polyphenol antioxidants will help to design more effective antioxidants for the treatment and prevention of diseases caused by metal-induced oxidative stress, as well as help to understand the structure–activity relationships of these compounds.

scholarly journals The ability of salts to inhibit the reaction between periodate anions and ovotransferrin

1986 ◽  
Vol 238 (3) ◽  
pp. 931-934 ◽  
Author(s):  
J J Hsuan
Keyword(s):  
Binding Site ◽  
Complex Anion ◽  
Anion Binding ◽  
Iron Binding ◽  
Binding Ability ◽  
Lyotropic Series

The reaction between periodate anions and apo-ovotransferrin results in the rapid abolition of the iron-binding ability of the protein and the loss of approximately 4 mol of tyrosine/mol of protein. The degree of inhibition exerted by a variety of salts on the rate of this reaction is found to be inconsistent with the lyotropic series and suggests the existence of a complex anion-binding site in the apoprotein. The existence of this site may explain the action of periodate anions on ovotransferrin.

Understanding Magnetite Biomineralisation: The Effect of Short Amino Acid Sequences on the {100} and the {111} Surface

2013 ◽  
Vol 1498 ◽  
pp. 239-245
Author(s):  
Amy E. Monnington ◽  
David J. Cooke
Keyword(s):  
Amino Acid ◽  
Glutamic Acid ◽  
Binding Sites ◽  
Amino Acid Sequences ◽  
Iron Binding ◽  
Binding Ability ◽  
C Terminus ◽  
Amino Acid Repeats ◽  
Magnetospirillum Magneticum ◽  
Magnetite Formation

ABSTRACTMagnetite (Fe3O4) formation within Magnetospirillum magneticum strain AMB-1 occurs under the influence of the Mms6 protein. It is hypothesised that if key iron binding sites within the C-terminus of the Mms6 protein are substituted for alanine, the protein’s overall iron binding ability is diminished. In this study, an atomistic model of Mms6-driven magnetite formation was developed and the attachment of series amino acid repeats (alanine-alanine, alanine-glutamic acid & glutamic acid-glutamic acid) to the {100} & {111} magnetite surfaces were investigated. Our results suggest the substitution of glutamic acid for alanine residues significantly reduces iron binding affinity of the system, thus confirming the hypothesis. In addition, it is shown that the surface of preferable attachment is the {111} magnetite surface.

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