Theoretical insights into the competitive metal bioaffinity of lactoferrin as a metal ion carrier: a DFT study

2019 ◽  
Vol 43 (41) ◽  
pp. 16374-16384 ◽  
Author(s):  
Bahareh Honarparvar ◽  
Suvardhan Kanchi ◽  
Krishna Bisetty
Keyword(s):  
Metal Ion ◽  
Protein Complexes ◽  
Body Fluids ◽  
Pivotal Role ◽  
Dft Study ◽  
Iron Binding ◽  
Ion Carrier ◽  
Living Organisms ◽  
Binding Glycoprotein

Metal–protein complexes, specifically lactoferrin (Lf), an iron-binding glycoprotein found naturally in milk and several other body fluids play a pivotal role in all living organisms.

scholarly journals Distribution of Lactoferrin Is Related with Dynamics of Neutrophils in Bacterial Infected Mice Intestine

Molecules ◽  
2020 ◽  
Vol 25 (7) ◽  
pp. 1496 ◽  
Author(s):  
Li Liang ◽  
Zhen-Jie Wang ◽  
Guang Ye ◽  
Xue-You Tang ◽  
Yuan-Yuan Zhang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Antimicrobial Activity ◽  
Mucosal Immunity ◽  
Mrna Levels ◽  
Iron Binding ◽  
E Coli ◽  
New Knowledge ◽  
Activated Neutrophils ◽  
Binding Glycoprotein

Lactoferrin (Lf) is a conserved iron-binding glycoprotein with antimicrobial activity, which is present in secretions that recover mucosal sites regarded as portals of invaded pathogens. Although numerous studies have focused on exogenous Lf, little is known about its expression of endogenous Lf upon bacterial infection. In this study, we investigated the distribution of Lf in mice intestine during Escherichia coli (E. coli) K88 infection. PCR and immunohistology staining showed that mRNA levels of Lf significantly increased in duodenum, ileum and colon, but extremely decreased in jejunum at 8 h and 24 h after infection. Meanwhile, endogenous Lf was mostly located in the lamina propria of intestine villi, while Lf receptor (LfR) was in the crypts. It suggested that endogenous Lf-LfR interaction might not be implicated in the antibacterial process. In addition, it was interesting to find that the infiltration of neutrophils into intestine tissues was changed similarly to Lf expression. It indicated that the variations of Lf expression were rather due to an equilibrium between the recruitment of neutrophils and degranulation of activated neutrophils. Thus, this new knowledge will pave the way to a more effective understanding of the role of Lf in intestinal mucosal immunity.

scholarly journals Diverse Mechanisms of Antimicrobial Activities of Lactoferrins, Lactoferricins, and Other Lactoferrin-Derived Peptides

2021 ◽  
Vol 22 (20) ◽  
pp. 11264
Author(s):  
Špela Gruden ◽  
Nataša Poklar Ulrih
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Molecular Level ◽  
Antioxidant Activities ◽  
Antimicrobial Activities ◽  
Iron Binding ◽  
Primary Focus ◽  
Binding Glycoprotein

Lactoferrins are an iron-binding glycoprotein that have important protective roles in the mammalian body through their numerous functions, which include antimicrobial, antitumor, anti-inflammatory, immunomodulatory, and antioxidant activities. Among these, their antimicrobial activity has been the most studied, although the mechanism behind antimicrobial activities remains to be elucidated. Thirty years ago, the first lactoferrin-derived peptide was isolated and showed higher antimicrobial activity than the native lactoferrin lactoferricin. Since then, numerous studies have investigated the antimicrobial potencies of lactoferrins, lactoferricins, and other lactoferrin-derived peptides to better understand their antimicrobial activities at the molecular level. This review defines the current antibacterial, antiviral, antifungal, and antiparasitic activities of lactoferrins, lactoferricins, and lactoferrin-derived peptides. The primary focus is on their different mechanisms of activity against bacteria, viruses, fungi, and parasites. The role of their structure, amino-acid composition, conformation, charge, hydrophobicity, and other factors that affect their mechanisms of antimicrobial activity are also reviewed.

Supported liquid membrane separation of propylene–propane mixtures using a metal ion carrier

Desalination ◽  
2010 ◽  
Vol 250 (1) ◽  
pp. 130-135 ◽  
Author(s):  
Maryam Takht Ravanchi ◽  
Tahereh Kaghazchi ◽  
Ali Kargari
Keyword(s):  
Metal Ion ◽  
Liquid Membrane ◽  
Membrane Separation ◽  
Supported Liquid Membrane ◽  
Ion Carrier

A DFT study on the metal ion selectivity of deferiprone complexes

2020 ◽  
Vol 86 ◽  
pp. 107267 ◽  
Author(s):  
Sadegh Kaviani ◽  
Mohammad Izadyar ◽  
Mohammad Reza Housaindokht
Keyword(s):  
Metal Ion ◽  
Ion Selectivity ◽  
Dft Study ◽  
Metal Ion Selectivity

scholarly journals Lactoferrin: A Modulator for Immunity against Tuberculosis Related Granulomatous Pathology

2015 ◽  
Vol 2015 ◽  
pp. 1-10 ◽  
Author(s):  
Jeffrey K. Actor
Keyword(s):  
Therapeutic Efficacy ◽  
Therapeutic Agent ◽  
Iron Binding ◽  
Therapeutic Tool ◽  
Cord Factor ◽  
Pulmonary Pathology ◽  
Mucosal Secretions ◽  
Binding Glycoprotein ◽  
Promising Avenue

There is great need for a therapeutic that would limit tuberculosis related pathology and thus curtail spread of disease between individuals by establishing a “firebreak” to slow transmission. A promising avenue to increase current therapeutic efficacy may be through incorporation of adjunct components that slow or stop development of aggressive destructive pulmonary pathology. Lactoferrin, an iron-binding glycoprotein found in mucosal secretions and granules of neutrophils, is just such a potential adjunct therapeutic agent. The focus of this review is to explore the utility of lactoferrin to serve as a therapeutic tool to investigate “disruption” of the mycobacterial granuloma. Proposed concepts for mechanisms underlying lactoferrin efficacy to control immunopathology are supported by data generated based onin vivomodels using nonpathogenic trehalose 6,6′-dimycolate (TDM, cord factor).

A quantum mechanical approach to ligand binding — Calculation of ligand–protein binding affinities for stromelysin-1 (MMP-3) inhibitors

2009 ◽  
Vol 87 (10) ◽  
pp. 1480-1484 ◽  
Author(s):  
Jian Li ◽  
Charles. H. Reynolds
Keyword(s):  
Ligand Binding ◽  
Metal Ion ◽  
Protein Complexes ◽  
Field Method ◽  
Binding Energies ◽  
Quantum Mechanical ◽  
Binding Affinities ◽  
Bond Forming ◽  
Proton Charge ◽  
Quantum Mechanical Approach

Linear-scaling quantum mechanical method was applied to calculate binding affinities of six stromelysin-1 (MMP-3) inhibitors with two different zinc binding groups (ZBGs). The entire protein and ligand–protein complexes were calculated using PM5 Hamiltonian, which enables the treatment of metal ion coordination, bond forming/breaking, and proton/charge transfers associated with the ligand binding process by the self-consistent field method. The calculated binding energies reproduce the binding-affinity trend observed experimentally.

Structural elucidation of a dual-activity PAP phosphatase-1 fromEntamoeba histolyticacapable of hydrolysing both 3′-phosphoadenosine 5′-phosphate and inositol 1,4-bisphosphate

2014 ◽  
Vol 70 (7) ◽  
pp. 2019-2031 ◽  
Author(s):  
Khaja Faisal Tarique ◽  
Syed Arif Abdul Rehman ◽  
S. Gourinath
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Genomic Analysis ◽  
Inositol Polyphosphate ◽  
Inositol Monophosphatase ◽  
Native Form ◽  
Catalytic Loop ◽  
Important Regulator ◽  
Living Organisms ◽  
Toxic Byproduct

The enzyme 3′-phosphoadenosine 5′-phosphatase-1 (PAP phosphatase-1) is a member of the Li+-sensitive Mg2+-dependent phosphatase superfamily, or inositol monophosphatase (IMPase) superfamily, and is an important regulator of the sulfate-activation pathway in all living organisms. Inhibition of this enzyme leads to accumulation of the toxic byproduct 3′-phosphoadenosine 5′-phosphate (PAP), which could be lethal to the organism. Genomic analysis ofEntamoeba histolyticasuggests the presence of two isoforms of PAP phosphatase. The PAP phosphatase-1 isoform of this organism is shown to be active over wide ranges of pH and temperature. Interestingly, this enzyme is inhibited by submillimolar concentrations of Li+, while being insensitive to Na+. Interestingly, the enzyme showed activity towards both PAP and inositol 1,4-bisphosphate and behaved as an inositol polyphosphate 1-phosphatase. Crystal structures of this enzyme in its native form and in complex with adenosine 5′-monophosphate have been determined to 2.1 and 2.6 Å resolution, respectively. The PAP phosphatase-1 structure is divided into two domains, namely α+β and α/β, and the substrate and metal ions bind between them. This is a first structure of any PAP phosphatase to be determined from a human parasitic protozoan. This enzyme appears to function using a mechanism involving three-metal-ion assisted catalysis. Comparison with other structures indicates that the sensitivity to alkali-metal ions may depend on the orientation of a specific catalytic loop.

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