Role of electrostatic interaction in the processes of complex formation

1987 ◽  
Vol 22 (5) ◽  
pp. 564-569
Author(s):  
P. A. Kondratenko
Keyword(s):  
Complex Formation ◽  
Electrostatic Interaction

scholarly journals An optical biosensor study of the interaction parameters and role of hydrophobic tails of cytochrome P450 2B4, b5 and NADPH-flavoprotein in complex formation

IUBMB Life ◽  
1997 ◽  
Vol 42 (4) ◽  
pp. 731-737 ◽  
Author(s):  
Yuriy Ivanov ◽  
Irina Kanaeva ◽  
Michail Eldarov ◽  
Konstantin Sklyabin ◽  
Michael Lehnerer ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Complex Formation ◽  
Optical Biosensor ◽  
Interaction Parameters ◽  
Cytochrome P450 2B4

scholarly journals Impact of Quantum Dot Surface on Complex Formation with Chlorin e6 and Photodynamic Therapy

Nanomaterials ◽  
2018 ◽  
Vol 9 (1) ◽  
pp. 9 ◽  
Author(s):  
Artiom Skripka ◽  
Dominyka Dapkute ◽  
Jurga Valanciunaite ◽  
Vitalijus Karabanovas ◽  
Ricardas Rotomskis
Keyword(s):  
Photodynamic Therapy ◽  
Cancer Therapy ◽  
Complex Formation ◽  
Chemical Properties ◽  
Disease Diagnosis ◽  
Chlorin E6 ◽  
Deep Tissue ◽  
Physico Chemical

Nanomaterials have permeated various fields of scientific research, including that of biomedicine, as alternatives for disease diagnosis and therapy. Among different structures, quantum dots (QDs) have distinctive physico-chemical properties sought after in cancer research and eradication. Within the context of cancer therapy, QDs serve the role of transporters and energy donors to photodynamic therapy (PDT) drugs, extending the applicability and efficiency of classic PDT. In contrast to conventional PDT agents, QDs’ surface can be designed to promote cellular targeting and internalization, while their spectral properties enable better light harvesting and deep-tissue use. Here, we investigate the possibility of complex formation between different amphiphilic coating bearing QDs and photosensitizer chlorin e6 (Ce6). We show that complex formation dynamics are dependent on the type of coating—phospholipids or amphiphilic polymers—as well as on the surface charge of QDs. Förster’s resonant energy transfer occurred in every complex studied, confirming the possibility of indirect Ce6 excitation. Nonetheless, in vitro PDT activity was restricted only to negative charge bearing QD-Ce6 complexes, correlating with better accumulation in cancer cells. Overall, these findings help to better design such and similar complexes, as gained insights can be straightforwardly translated to other types of nanostructures—expanding the palette of possible therapeutic agents for cancer therapy.

scholarly journals Iron Requirement for Mn(II) Oxidation by Leptothrix discophora SS-1

2008 ◽  
Vol 75 (5) ◽  
pp. 1229-1235 ◽  
Author(s):  
Iman A. El Gheriany ◽  
Daniela Bocioaga ◽  
Anthony G. Hay ◽  
William C. Ghiorse ◽  
Michael L. Shuler ◽  
...  
Keyword(s):  
Complex Formation ◽  
Temporal Variations ◽  
Iron Limitation ◽  
Gene Transcript ◽  
Cellular Functions ◽  
Transcript Levels ◽  
Leptothrix Discophora ◽  
Geochemical Cycling ◽  
Iron Requirement

ABSTRACT A common form of biocatalysis of Mn(II) oxidation results in the formation of biogenic Mn(III, IV) oxides and is a key reaction in the geochemical cycling of Mn. In this study, we grew the model Mn(II)-oxidizing bacterium Leptothrix discophora SS-1 in media with limited iron (0.1 μM iron/5.8 mM pyruvate) and sufficient iron (0.2 μM iron/5.8 mM pyruvate). The influence of iron on the rate of extracellular Mn(II) oxidation was evaluated. Cultures in which cell growth was limited by iron exhibited reduced abilities to oxidize Mn(II) compared to cultures in medium with sufficient iron. While the extracellular Mn(II)-oxidizing factor (MOF) is thought to be a putative multicopper oxidase, Mn(II) oxidation in the presence of zero added Cu(II) was detected and the decrease in the observed Mn(II) oxidation rate in iron-limited cultures was not relieved when the medium was supplemented with Cu(II). The decline of Mn(II) oxidation under iron-limited conditions was not accompanied by siderophore production and is unlikely to be an artifact of siderophore complex formation with Mn(III). The temporal variations in mofA gene transcript levels under conditions of limited and abundant iron were similar, indicating that iron limitation did not interfere with the transcription of the mofA gene. Our quantitative PCR results provide a step forward in understanding the regulation of Mn(II) oxidation. The mechanistic role of iron in Mn(II) oxidation is uncertain; the data are consistent with a direct requirement for iron as a component of the MOF or an indirect effect of iron resulting from the limitation of one of many cellular functions requiring iron.

Essential role of amino acids in αD–β4 loop of a Bacillus thuringiensis Cyt2Aa2 toxin in binding and complex formation on lipid membrane

Toxicon ◽  
2013 ◽  
Vol 74 ◽  
pp. 130-137 ◽  
Author(s):  
Kunat Suktham ◽  
Wanwarang Pathaichindachote ◽  
Boonhiang Promdonkoy ◽  
Chartchai Krittanai
Keyword(s):  
Amino Acids ◽  
Bacillus Thuringiensis ◽  
Complex Formation ◽  
Essential Role ◽  
Lipid Membrane

Self-Assembly of Alkali Lignin in Tetrahydrofuran

2012 ◽  
Vol 550-553 ◽  
pp. 57-61
Author(s):  
Hao Li ◽  
Yong Hong Deng ◽  
Kai Huang
Keyword(s):  
Charge Transfer ◽  
Electrostatic Interaction ◽  
Self Assembly ◽  
The Self ◽  
Charge Transfer Complexes ◽  
Layer By Layer ◽  
Alkali Lignin ◽  
Higher Temperature ◽  
Effects Of Temperature

Alkali lignin (AL) was used as a polyanion to form layer-by-layer self-assembled film with PDAC as a polycation. The effects of temperature and concentration on the adsorption characteristics of AL were investigated. Iodine was added into AL solutions to study the role of π-π interaction in self-assembly of AL and PDAC. Results show that the self-assembly of AL/PDAC is mainly driven by π-π interaction and electrostatic interaction. A higher temperature or a larger concentration can enhance the aggregation of lignin. I2 can form lignin–iodine charge–transfer complexes with AL to reduce the degree of aggregation of AL, so the adsorbed amount of AL decreases significantly with increasing iodine contents.

scholarly journals Genetic Analysis of Human Chymotrypsin-Like Elastases 3A and 3B (CELA3A and CELA3B) to Assess the Role of Complex Formation between Proelastases and Procarboxypeptidases in Chronic Pancreatitis

Pancreatology ◽  
2017 ◽  
Vol 17 (3) ◽  
pp. S28
Author(s):  
Andrea Parniczky ◽  
Eszter Hegyi ◽  
Anna Zsófia Tóth ◽  
Ákos Szücs ◽  
Andrea Szentesi ◽  
...  
Keyword(s):  
Chronic Pancreatitis ◽  
Complex Formation ◽  
Genetic Analysis

Essential role of human CDT1 in DNA replication and chromatin licensing

2002 ◽  
Vol 115 (7) ◽  
pp. 1435-1440 ◽  
Author(s):  
Mickael Rialland ◽  
Francesco Sola ◽  
Corrado Santocanale
Keyword(s):  
Cell Cycle ◽  
Dna Replication ◽  
Complex Formation ◽  
Fission Yeast ◽  
Origin Recognition Complex ◽  
Essential Role ◽  
Large Body ◽  
Transformed Cells ◽  
Minichromosome Maintenance

Formation of pre-replicative complexes at origins is an early cell cycle event essential for DNA duplication. A large body of evidence supports the notion that Cdc6 protein, through its interaction with the origin recognition complex, is required for pre-replicative complex assembly by loading minichromosome maintenance proteins onto DNA. In fission yeast and Xenopus, this reaction known as the licensing of chromatin for DNA replication also requires the newly identified Cdt1 protein. We studied the role of hCdt1 protein in the duplication of the human genome by antibody microinjection experiments and analyzed its expression during the cell cycle in human non-transformed cells. We show that hCdt1 is essential for DNA replication in intact human cells, that it executes its function in a window of the cell cycle overlapping with pre-replicative complex formation and that it is necessary for the loading of minichromosome maintenance proteins onto chromatin. Intriguingly, we observed that hCdt1 protein, in contrast to other licensing factors, is already present in serum-deprived G0 arrested cells and its levels increase only marginally upon re-entry in the cell cycle.

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