scholarly journals Factors governing the competition between group IA and IB cations for monensin A: a DFT/PCM study

RSC Advances ◽  
2020 ◽  
Vol 10 (10) ◽  
pp. 5734-5741
Author(s):  
Todor Dudev ◽  
Diana Cheshmedzhieva ◽  
Radoslava Dimitrova ◽  
Peter Dorkov ◽  
Ivayla Pantcheva
Keyword(s):  
Metal Selectivity ◽  
Monensin A

The results obtained suggest that the metal selectivity of monensin can be modulated by changing the solvents used.

Molecular structure of the 1:1 inclusion complex of monensin A sodium salt with acetonitrile

2007 ◽  
Vol 832 (1-3) ◽  
pp. 84-89 ◽  
Author(s):  
Adam Huczyński ◽  
Małgorzata Ratajczak-Sitarz ◽  
Andrzej Katrusiak ◽  
Bogumil Brzezinski
Keyword(s):  
Molecular Structure ◽  
Inclusion Complex ◽  
Sodium Salt ◽  
Monensin A

Contractile responses to ouabain and K+-free solution in aorta from hypertensive rats

1986 ◽  
Vol 250 (4) ◽  
pp. H612-H619 ◽  
Author(s):  
R. S. Moreland ◽  
T. C. Major ◽  
R. C. Webb
Keyword(s):  
Channel Blocker ◽  
Isometric Force ◽  
Maximal Response ◽  
Na Channel ◽  
Free Solution ◽  
Contractile Responses ◽  
Spontaneously Hypertensive ◽  
Force Development ◽  
Monensin A ◽  
Wistar Kyoto

This study characterizes isometric force development in response to ouabain and K+-free solution in isolated aortic strips from spontaneously hypertensive (SHR) and Wistar-Kyoto (WKY) rats. SHR aortas were more sensitive to ouabain than those from WKY (threshold: SHR, 3.1 X 10(-5) M; WKY, 25.6 X 10(-5) M), and force development in response to 10(-3) M ouabain was greater in SHR (SHR, 586 +/- 51 mg; WKY, 245 +/- 24 mg). Monensin, a Na+ ionophore, potentiated contractile responses to ouabain, whereas amiloride, a Na+ channel blocker, and low Na+ solutions depressed contractile responses to ouabain. Contractile responses of SHR aortic strips to K+-free solution were faster than those of WKY aortic strips [time to half-maximal response (t1/2): SHR, 24 +/- 5 min; WKY, 47 +/- 4 min]. Maximal force development by aortic strips from SHR in response to K+-free solution was not different from that of WKY aortic strips (SHR, 808 +/- 34 mg; WKY, 750 +/- 37 mg). Monensin (10(-5) M) increased the rate of force development to K+-free solution to a greater extent in WKY aortic strips than in those from SHR (t1/2: SHR, 3 +/- 1 min; WKY, 4 +/- 2 min). Amiloride and low Na+ solution depressed contractile responses to K+-free solution in both SHR and WKY aortic strips. These observations demonstrate that SHR aortas are more responsive to ouabain and K+-free solution compared with WKY aortas. Contractile responses to ouabain and K+-free solution were sensitive to experimental interventions that alter transmembrane Na+ movements.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals European field evaluation of monensin, a new anticoccidial agent

1974 ◽  
Vol 3 (1) ◽  
pp. 25-35 ◽  
Author(s):  
M.L. Clarke ◽  
M. Diaz ◽  
B. Guilloteau ◽  
P.L Hudd ◽  
J.W. Stoker
Keyword(s):  
Field Evaluation ◽  
Monensin A ◽  
Anticoccidial Agent

scholarly journals Cytosolic Ni(II) Sensor in Cyanobacterium

2012 ◽  
Vol 287 (15) ◽  
pp. 12142-12151 ◽  
Author(s):  
Andrew W. Foster ◽  
Carl J. Patterson ◽  
Rafael Pernil ◽  
Corinna R. Hess ◽  
Nigel J. Robinson
Keyword(s):  
Coordination Sphere ◽  
Promoter Region ◽  
Nitrilotriacetic Acid ◽  
The Other ◽  
Cryptic Promoter ◽  
Difference Spectra ◽  
Inner Membrane ◽  
Fura 2 ◽  
Metal Selectivity ◽  
Metal Sensors

Efflux of surplus Ni(II) across the outer and inner membranes of Synechocystis PCC 6803 is mediated by the Nrs system under the control of a sensor of periplasmic Ni(II), NrsS. Here, we show that the product of ORF sll0176, which encodes a CsoR/RcnR-like protein now designated InrS (for internal nickel-responsive sensor), represses nrsD (NrsD is deduced to efflux Ni(II) across the inner membrane) from a cryptic promoter between the final two ORFs in the nrs operon. Transcripts initiated from the newly identified nrsD promoter accumulate in response to nickel or cobalt but not copper, and recombinant InrS forms specific, Ni(II)-inhibited complexes with the nrsD promoter region. Metal-dependent difference spectra of Ni(II)- and Cu(I)-InrS are similar to Cu(I)-sensing CsoR and dissimilar to Ni(II)/Co(II)-sensing RcnR, consistent with factors beyond the primary coordination sphere switching metal selectivity. Competition with chelators mag-fura-2, nitrilotriacetic acid, EDTA, and EGTA estimate KD Ni(II) for the tightest site of InrS as 2.05 (±1.5) × 10−14m, and weaker KD Ni(II) for the cells' metal sensors of other types: Zn(II) co-repressor Zur, Co(II) activator CoaR, and Zn(II) derepressor ZiaR. Ni(II) transfer to InrS occurs upon addition to Ni(II) forms of each other sensor. InrS binds Ni(II) sufficiently tightly to derepress Ni(II) export at concentrations below KD Ni(II) of the other sensors.

scholarly journals Structure and Antimicrobial Properties of Monensin A and Its Derivatives: Summary of the Achievements

2013 ◽  
Vol 2013 ◽  
pp. 1-14 ◽  
Author(s):  
Daniel Łowicki ◽  
Adam Huczyński
Keyword(s):  
Antimicrobial Activity ◽  
Lipid Membranes ◽  
Antimicrobial Properties ◽  
Biological Properties ◽  
Sodium Cation ◽  
Hydroxyl Groups ◽  
Carboxyl Group ◽  
Growth Promoter ◽  
Monensin A

In this paper structural and microbiological studies on the ionophorous antibiotic monensin A and its derivatives have been collected. Monensin A is an ionophore which selectively complexes and transports sodium cation across lipid membranes, and therefore it shows a variety of biological properties. This antibiotic is commonly used as coccidiostat and nonhormonal growth promoter. The paper focuses on both the latest and earlier achievements concerning monensin A antimicrobial activity. The activities of monensin derivatives, including modifications of hydroxyl groups and carboxyl group, are also presented.

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