scholarly journals Potentiometric and Blood Plasma Simulation Studies of Nickel(II) Complexes of Poly(amino)amido Pentadentate Ligands: Computer Aided Metal-Based Drug Design

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Sebusi Odisitse ◽  
Graham E. Jackson

The thermodynamic equilibria of nickel(II) with N,N′-di(aminoethylene)-2,6-pyridinedicarbonylamine (L1), Bis-(N,N-dimethylethyl)-2,6-pyridinedicarboxamide (L2), and N,N′-bis[2(2-pyridyl)-methyl]pyridine-2,6-dicarboxamide (L3) have been studied at 25°C and an ionic strength of 0.15 mol dm−3by glass electrode potentiometry. The protonation and formation constants added to blood plasma model predict that Cu(II) competes effectively against Ni(II), Zn(II), and Ca(II) for these ligandsin vivo.

2000 ◽  
Vol 53 (5) ◽  
pp. 369 ◽  
Author(s):  
Faradj K. Samani ◽  
Stephen G. Capewell ◽  
Pal M. Sipos ◽  
Peter M. May ◽  
Glenn Hefter

The ionic product of water, pKw = –log[H+][OH–], has been determined as a function of ionic strength (I ) in concentrated aqueous solutions of KCl, KBr and KI at 25˚C by high-precision glass electrode potentiometric titrations. The pKw values obtained are in excellent agreement with, but generally more precise than, literature data. At I > 1 M the pKw values increase smoothly and show systematic differences in the order KCl < KBr < KI, consistent with the decreasing H+-acceptor ability of the medium anions. Analogous behaviour is observed in MCl solutions, with pKw values varying in the order NaCl < KCl < CsCl. Formation constants of MOH0 ion pairs derived from these data are consistent with literature values.


1995 ◽  
Vol 48 (7) ◽  
pp. 1283 ◽  
Author(s):  
JS Solis ◽  
G Hefter ◽  
PM May

Chemical speciation in the system CuI/NH3/Cl- which may be represented by the general equilibrium pCuI(aq)+qNH3(aq)+rCl-(aq)↔ Cup(NH3)qClr(p-r)+(aq) has been studied by glass electrode potentiometry at 25.0°C and an ionic strength of 1.00 M (NaClO4). A number of binary and ternary complexes were detected with formation constants, βpqr: logβ120 = 11.381�0.077, logβ111 = 8.920�0.045, logβ112 = 8.82�0.18 and logβ121 = 11.33�0.24. The ionization constant of water (pKw) and the protonation constant of ammonia (pKa) obtained by the same procedures were 13.7462�0.0012 and 9.4613�0.0010 at I = 1 (NaClO4), and 13.7165�0.0010 and 9.4521�0.0007 at I = 1 (NaCl) respectively.


Author(s):  
Greg V. Martin ◽  
Ann L. Hubbard

The microtubule (MT) cytoskeleton is necessary for many of the polarized functions of hepatocytes. Among the functions dependent on the MT-based cytoskeleton are polarized secretion of proteins, delivery of endocytosed material to lysosomes, and transcytosis of integral plasma membrane (PM) proteins. Although microtubules have been shown to be crucial to the establishment and maintenance of functional and structural polarization in the hepatocyte, little is known about the architecture of the hepatocyte MT cytoskeleton in vivo, particularly with regard to its relationship to PM domains and membranous organelles. Using an in situ extraction technique that preserves both microtubules and cellular membranes, we have developed a protocol for immunofluorescent co-localization of cytoskeletal elements and integral membrane proteins within 20 µm cryosections of fixed rat liver. Computer-aided 3D reconstruction of multi-spectral confocal microscope images was used to visualize the spatial relationships among the MT cytoskeleton, PM domains and intracellular organelles.


1992 ◽  
Vol 38 (4) ◽  
pp. 562-565 ◽  
Author(s):  
M A Kline ◽  
C Orvig

Abstract The stability constants for the Fe(III) complexes of the orally active iron decorporation drug L1 (3-hydroxy-1,2-dimethyl-4-pyridinone) have been determined by potentiometric titration [glass electrode, 25.0 degrees C, mu = 0.15 mol/L (isotonic) NaCl]. A simple computer model of blood plasma (citrate 100 mumol/L, transferrin 37 mumol/L) has been used to compare the Fe(III) binding efficacies in blood of L1 and the clinically used intravenously administered chelating agent deferoxamine.


1980 ◽  
Vol 186 (2) ◽  
pp. 591-598 ◽  
Author(s):  
Christopher Kirby ◽  
Jacqui Clarke ◽  
Gregory Gregoriadis

Small unilamellar neutral, negatively and positively charged liposomes composed of egg phosphatidylcholine, various amounts of cholesterol and, when appropriate, phosphatidic acid or stearylamine and containing 6-carboxyfluorescein were injected into mice, incubated with mouse whole blood, plasma or serum or stored at 4°C. Liposomal stability, i.e. the extent to which 6-carboxyfluorescein is retained by liposomes, was dependent on their cholesterol content. (1) Cholesterol-rich (egg phosphatidylcholine/cholesterol, 7:7 molar ratio) liposomes, regardless of surface charge, remained stable in the blood of intravenously injected animals for up to at least 400min. In addition, stability of cholesterol-rich liposomes was largely maintained in vitro in the presence of whole blood, plasma or serum for at least 90min. (2) Cholesterol-poor (egg phosphatidylcholine/cholesterol, 7:2 molar ratio) or cholesterol-free (egg phosphatidylcholine) liposomes lost very rapidly (at most within 2min) much of their stability after intravenous injection or upon contact with whole blood, plasma or serum. Whole blood and to some extent plasma were less detrimental to stability than was serum. (3) After intraperitoneal injection, neutral cholesterol-rich liposomes survived in the peritoneal cavity to enter the blood circulation in their intact form. Liposomes injected intramuscularly also entered the circulation, although with somewhat diminished stability. (4) Stability of neutral and negatively charged cholesterol-rich liposomes stored at 4°C was maintained for several days, and by 53 days it had declined only moderately. Stored liposomes retained their unilamellar structure and their ability to remain stable in the blood after intravenous injection. (5) Control of liposomal stability by adjusting their cholesterol content may help in the design of liposomes for effective use in biological systems in vivo and in vitro.


1965 ◽  
Vol 20 (6) ◽  
pp. 1332-1336 ◽  
Author(s):  
Edward W. Moore ◽  
James W. Ross

In the investigation of numerous physiological phenomena it is the activity of an ion species which is desired, rather than stoichiometric concentration. The calculation of mean ionic activity from known concentration data requires accurate activity coefficients (ggr). This report concerns the determination of ggrNaCl and ggrCaCl2 in mixed NaCl-CaCl2 solutions by potentiometric measurement with a sodium-selective glass electrode-Ag/AgCl electrode system over the ionic strength range 0.05–0.5 m. Log ggrNaCl varied linearly, at constant total ionic strength, with the ionic strength of CaCl2 in the mixture, in accordance with Harned's rule. From data thus obtained, ggrCaCl2 coefficients in such mixed solutions have been calculated and compared with values calculated from published osmotic data. Resulting activity coefficient curves for ggrCaCl2 are presented over the concentration range encountered in serum and other extracellular fluids. Note: (With the Technical Assistance of Leonard Kaye and Leonard L. Anderson) glass electrodes; ion interaction; electrolyte metabolism; Harned's rule; membrane transport; osmotic coefficients Submitted on March 11, 1965


2020 ◽  
Author(s):  
Jae Myoung Suh ◽  
Kwang-eun Kim ◽  
Isaac Park ◽  
Jeesoo Kim ◽  
Myeong-Gyun Kang ◽  
...  

Abstract Here we describe iSLET (in situ Secretory protein Labeling via ER-anchored TurboID) which labels secretory pathway proteins as they transit through the ER-lumen to enable dynamic tracking of tissue-specific secreted proteomes in vivo. We expressed iSLET in the mouse liver and demonstrated efficient in situ labeling of the liver-specific secreted proteome which could be tracked and identified within circulating blood plasma. iSLET is a versatile and powerful tool for studying spatiotemporal dynamics of secretory proteins, a valuable class of biomarkers and therapeutic targets.


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