Activity of NADH oxidase from Thermus thermophilus in water/alcohol binary mixtures is limited by the stability of quaternary structure

2010 ◽  
Vol 64 (1-2) ◽  
pp. 60-67 ◽  
Author(s):  
Kamil Tóth ◽  
Erik Sedlák ◽  
Andrej Musatov ◽  
Gabriel Žoldák
Biomolecules ◽  
2019 ◽  
Vol 9 (4) ◽  
pp. 128 ◽  
Author(s):  
Fredrick Nwude Eze ◽  
Ladda Leelawatwattana ◽  
Porntip Prapunpoj

Transthyretin is responsible for a series of highly progressive, degenerative, debilitating, and incurable protein misfolding disorders known as transthyretin (TTR) amyloidosis. Since dissociation of the homotetrameric protein to its monomers is crucial in its amyloidogenesis, stabilizing the native tetramer from dissociating using small-molecule ligands has proven a viable therapeutic strategy. The objective of this study was to determine the potential role of the medicinal herb Centella asiatica on human transthyretin (huTTR) amyloidogenesis. Thus, we investigated the stability of huTTR with or without a hydrophilic fraction of C. asiatica (CAB) against acid/urea-mediated denaturation. We also determined the influence of CAB on huTTR fibrillation using transmission electron microscopy. The potential binding interactions between CAB and huTTR was ascertained by nitroblue tetrazolium redox-cycling and 8-anilino-1-naphthalene sulfonic acid displacement assays. Additionally, the chemical profile of CAB was determined by liquid chromatography quadruple time-of-flight mass spectrometry (HPLC-QTOF-MS). Our results strongly suggest that CAB bound to and preserved the quaternary structure of huTTR in vitro. CAB also prevented transthyretin fibrillation, although aggregate formation was unmitigated. These effects could be attributable to the presence of phenolics and terpenoids in CAB. Our findings suggest that C. asiatica contains pharmaceutically relevant bioactive compounds which could be exploited for therapeutic development against TTR amyloidosis.


1980 ◽  
Vol 7 (1) ◽  
pp. 109-118 ◽  
Author(s):  
E. Nagy ◽  
O. Borlai ◽  
A. Ujhidy

2010 ◽  
Vol 2010 ◽  
pp. 1-7 ◽  
Author(s):  
Liron Klipcan ◽  
Igal Finarov ◽  
Nina Moor ◽  
Mark G. Safro

Aminoacyl-tRNA synthetases (aaRSs) are a canonical set of enzymes that specifically attach corresponding amino acids to their cognate transfer RNAs in the cytoplasm, mitochondria, and nucleus. The aaRSs display great differences in primary sequence, subunit size, and quaternary structure. Existence of three types of phenylalanyl-tRNA synthetase (PheRS)—bacterial (αβ)2, eukaryotic/archaeal cytosolic (αβ)2, and mitochondrial α—is a prominent example of structural diversity within the aaRSs family. Although archaeal/eukaryotic and bacterial PheRSs share common topology of the core domains and the B3/B4 interface, where editing activity of heterotetrameric PheRSs is localized, the detailed investigation of the three-dimensional structures from three kingdoms revealed significant variations in the local design of their synthetic and editing sites. Moreover, as might be expected from structural data eubacterial, Thermus thermophilus and human cytoplasmic PheRSs acquire different patterns of tRNAPhe anticodon recognition.


1994 ◽  
Vol 3 (11) ◽  
pp. 1998-2004 ◽  
Author(s):  
Patrick Tauc ◽  
Richard T. Keiser ◽  
Evan R. Kantrowitz ◽  
Patrice Vachette

2011 ◽  
Vol 51 (1-2) ◽  
pp. 71-82 ◽  
Author(s):  
Teresa Miletti ◽  
Patrick J. Farber ◽  
Anthony Mittermaier

1995 ◽  
Vol 2 (12) ◽  
pp. 1109-1114 ◽  
Author(s):  
H.J. Hecht ◽  
H. Erdmann ◽  
H.J. Park ◽  
M. Sprinzl ◽  
R.D. Schmid

1994 ◽  
Vol 668 (1) ◽  
pp. 153-164 ◽  
Author(s):  
J. Kirchberger ◽  
H. Erdmann ◽  
H.-J. Hecht ◽  
G. Kopperschläger

Author(s):  
Eva Valušová ◽  
Erik Sedlák ◽  
Marián Antalík ◽  
Steffen Nock ◽  
Mathias Sprinzl

2012 ◽  
Vol 62 (4) ◽  
pp. 515-528 ◽  
Author(s):  
Tanja Vehovec ◽  
Andrej Gartner ◽  
Odon Planinšek ◽  
Aleš Obreza

Influence of some commercially available types of microcrystalline cellulose (MCC) on the stability of certain active pharmaceutical ingredients (APIs), when in contact, has been investigated. Two structurally similar APIs, perindopril erbumine (PER) and enalapril maleate (EM), both well-known angiotensin-converting enzyme inhibitors were used. The main properties of an MCC that could determine the stability for each API were measured and correlated to the stability of these two APIs in binary mixtures. The stability of these APIs differed when in contact with different types of MCC. The dominant properties of MCC from one manufacturer were surface features that influenced the stability of PER and acidity that influenced the stability of EM. In the case of MCC from other manufacturers, unbound water was stability determining for both substances.


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