3 research outputs found
Multiple and Variable Binding of Pharmacologically Active Bis(maltolato)oxidovanadium(IV) to Lysozyme
The interaction with
proteins of metal-based drugs plays a crucial
role in their transport, mechanism, and activity. For an active MLn complex, where L is the organic carrier,
various binding modes (covalent and non-covalent, single or multiple)
may occur and several metal moieties (M, ML, ML2, etc.)
may interact with proteins. In this study, we have evaluated the interaction
of [VIVOÂ(malt)2] (bisÂ(maltolato)ÂoxidovanadiumÂ(IV)
or BMOV, where malt = maltolato, i.e., the common name for 3-hydroxy-2-methyl-4H-pyran-4-onato) with the model protein hen egg white lysozyme
(HEWL) by electrospray ionization mass spectrometry, electron paramagnetic
resonance, and X-ray crystallography. The multiple binding of different
V-containing isomers and enantiomers to different sites of HEWL is
observed. The data indicate both non-covalent binding of cis-[VOÂ(malt)2(H2O)] and [VOÂ(malt)Â(H2O)3]+ and covalent binding of [VOÂ(H2O)3â4]2+ and cis-[VOÂ(malt)2] and other V-containing fragments to the side chains of Glu35,
Asp48, Asn65, Asp87, and Asp119 and to the C-terminal carboxylate.
Our results suggest that the multiple and variable interactions of
potential VIVOL2 drugs with proteins can help
to better understand their solution chemistry and contribute to define
the molecular basis of the mechanism of action of these intriguing
molecules
Effect of Equatorial Ligand Substitution on the Reactivity with Proteins of Paddlewheel Diruthenium Complexes: Structural Studies
The paddlewheel [Ru2Cl(O2CCH3)4] complex was previously reported to react with
the model
protein hen egg white lysozyme (HEWL), forming adducts with two diruthenium
moieties bound to Asp101 and Asp119 side chains upon the release of
one acetate. To study the effect of the equatorial ligands on the
reactivity with proteins of diruthenium compounds, X-ray structures
of the adducts formed when HEWL reacts with [Ru2Cl(D-p-FPhF)(O2CCH3)3] [D-p-FPhF = N,Nâ˛-bis(4-fluorophenyl)formamidinate]
under different conditions were solved. [Ru2Cl(D-p-FPhF)(O2CCH3)3] is bonded
through their equatorial positions to the Asp side chains. Protein
binding occurs cis or trans to D-p-FPhF. Lys or Arg
side chains or even main-chain carbonyl groups can coordinate to the
diruthenium core at the axial site. Data help to understand the reactivity
of paddlewheel diruthenium complexes with proteins, providing useful
information for the design of new artificial diruthenium-containing
metalloenzymes with potential applications in the fields of catalysis,
biomedicine, and biotechnology
Inside out <i>Porphyridium cruentum</i>: Beyond the Conventional Biorefinery Concept
Here, an unprecedented
biorefinery approach has been designed to
recover high-added value bioproducts starting from the culture ofPorphyridium cruentum. This unicellular marine red
alga can secrete and accumulate high-value compounds that can find
applications in a wide variety of industrial fields. 300 Âą 67
mg/L of exopolysaccharides were obtained from cell culture medium;
phycoerythrin was efficiently extracted (40% of total extract) and
isolated by single chromatography, with a purity grade that allowed
the crystal structure determination at 1.60 Ă
; a twofold increase
in β-carotene yield was obtained from the residual biomass;
the final residual biomass was found to be enriched in saturated fatty
acids. Thus, for the first time, a complete exploitation ofP. cruentumculture was set up