scholarly journals Weak protein–cationic co-ion interactions addressed by X-ray crystallography and mass spectrometry

2014 ◽  
Vol 70 (8) ◽  
pp. 2217-2231 ◽  
Author(s):  
Philippe Bénas ◽  
Nicolas Auzeil ◽  
Laurent Legrand ◽  
Franck Brachet ◽  
Anne Regazzetti ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Protein Solubility ◽  
Ionization Mass ◽  
X Ray ◽  
Esi Ms ◽  
X Ray Crystallography ◽  
Egg White Lysozyme ◽  
Ion Interactions ◽  
Carboxylic Groups ◽  
Hen Egg White

The adsorption of Rb+, Cs+, Mn2+, Co2+and Yb3+onto the positively charged hen egg-white lysozyme (HEWL) has been investigated by solving 13 X-ray structures of HEWL crystallized with their chlorides and by applying electrospray ionization mass spectrometry (ESI-MS) first to dissolved protein crystals and then to the protein in buffered salt solutions. The number of bound cations follows the order Cs+< Mn2+≃ Co2+< Yb3+at 293 K. HEWL binds less Rb+(qtot= 0.7) than Cs+(qtot= 3.9) at 100 K. Crystal flash-cooling drastically increases the binding of Cs+, but poorly affects that of Yb3+, suggesting different interactions. The addition of glycerol increases the number of bound Yb3+cations, but only slightly increases that of Rb+. HEWL titrations with the same chlorides, followed by ESI-MS analysis, show that only about 10% of HEWL binds Cs+and about 40% binds 1–2 Yb3+cations, while the highest binding reaches 60–70% for protein binding 1–3 Mn2+or Co2+cations. The binding sites identified by X-ray crystallography show that the monovalent Rb+and Cs+preferentially bind to carbonyl groups, whereas the multivalent Mn2+, Co2+and Yb3+interact with carboxylic groups. This work elucidates the basis of the effect of the Hofmeister cation series on protein solubility.

scholarly journals Reaction with Proteins of a Five-Coordinate Platinum(II) Compound

2019 ◽  
Vol 20 (3) ◽  
pp. 520 ◽  
Author(s):  
Giarita Ferraro ◽  
Tiziano Marzo ◽  
Maria Cucciolito ◽  
Francesco Ruffo ◽  
Luigi Messori ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Platinum Complexes ◽  
Rnase A ◽  
Side Chain ◽  
Planar Geometry ◽  
Ionization Mass ◽  
X Ray ◽  
X Ray Crystallography ◽  
Egg White Lysozyme ◽  
Square Planar

Stable five-coordinate Pt(II) complexes have been highlighted as a promising and original platform for the development of new cytotoxic drugs. Their interaction with proteins has been scarcely studied. Here, the reactivity of the five-coordinate Pt(II) compound [Pt(I)(Me) (dmphen)(olefin)] (Me = methyl, dmphen = 2,9-dimethyl-1,10-phenanthroline, olefin = dimethylfumarate) with the model proteins hen egg white lysozyme (HEWL) and bovine pancreatic ribonuclease (RNase A) has been investigated by X-ray crystallography and electrospray ionization mass spectrometry. The X-ray structures of the adducts of RNase A and HEWL with [Pt(I)(Me)(dmphen)(olefin)] are not of very high quality, but overall data indicate that, upon reaction with RNase A, the compound coordinates the side chain of His105 upon releasing the iodide ligand, but retains the pentacoordination. On the contrary, upon reaction with HEWL, the trigonal bi-pyramidal Pt geometry is lost, the iodide and the olefin ligands are released, and the metal center coordinates the side chain of His15 probably adopting a nearly square-planar geometry. This work underlines the importance of the combined use of crystallographic and mass spectrometry techniques to characterize, in detail, the protein–metallodrug recognition process. Our findings also suggest that five-coordinate Pt(II) complexes can act either retaining their uncommon structure or functioning as prodrugs, i.e., releasing square-planar platinum complexes as bioactive species.

scholarly journals Synthesis, Crystal Structure and Interaction with Bovine Serum Albumin (BSA) of Two α-Aminophosphonic Acids Derivatives

2019 ◽  
pp. 1-7
Author(s):  
Wei Huang ◽  
Wen-Ling Wang
Keyword(s):  
Crystal Structure ◽  
Mass Spectrometry ◽  
Binding Constants ◽  
Ionization Mass ◽  
Monoclinic System ◽  
X Ray ◽  
X Ray Crystallography ◽  
Aminophosphonic Acids ◽  
Amino Phosphonate ◽  
Ft Ir

Two α-amino-phosphonate derivatives (1 & 2) were synthesized and their compositions and structures were characterized by Elemental Analysis (EA), FT-IR Spectrascopy (FT-IR), Electrospray Ionization Mass Spectrometry (ESI-MS), Nuclear Magnetic Resonance (NMR, 1H, 13C and 31P) and X-ray crystallography. Compound 1 & 2 were crystallized in monoclinic system with the space group P2(1)/n and P2(1)/c, respectively. The interaction effects of two α-aminophosphonate derivatives (1 & 2) with BSA were investigated and the binding constants were 1.07 × 104 M-1, 1.68 × 104 M-1, respectively. Besides, the values of n were indicated that 1:1 complex was formed between BSA and 1&2.

The metalation of hen egg white lysozyme impacts protein stability as shown by ion mobility mass spectrometry, differential scanning calorimetry, and X-ray crystallography

2017 ◽  
Vol 53 (30) ◽  
pp. 4246-4249 ◽  
Author(s):  
Matthew P. Sullivan ◽  
Michael Groessl ◽  
Samuel M. Meier ◽  
Richard L. Kingston ◽  
David C. Goldstone ◽  
...  
Keyword(s):  
Ion Mobility ◽  
Egg White ◽  
Ion Mobility Mass Spectrometry ◽  
Hen Egg White Lysozyme ◽  
Scanning Calorimetry ◽  
X Ray ◽  
X Ray Crystallography ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hen Egg

Metalation of lysozyme with anticancer organometallics results in protein destabilisation, probably relevant in metallodrug mode of action.

Combined analysis of 1,3-benzodioxoles by crystalline sponge X-ray crystallography and laser desorption ionization mass spectrometry

The Analyst ◽  
2018 ◽  
Vol 143 (6) ◽  
pp. 1475-1481 ◽  
Author(s):  
Yukako Hayashi ◽  
Kazuaki Ohara ◽  
Rika Taki ◽  
Tomomi Saeki ◽  
Kentaro Yamaguchi
Keyword(s):  
Mass Spectrometry ◽  
Laser Desorption ◽  
Promising Method ◽  
Ionization Mass Spectrometry ◽  
Ionization Mass ◽  
Laser Desorption Ionization ◽  
Combined Analysis ◽  
X Ray ◽  
X Ray Crystallography ◽  
Desorption Ionization

The combination of X-ray analysis and laser desorption ionization by using crystalline sponge will be a promising method to determine guest structures.

scholarly journals Syntheses and Reactivity of New Zwitterionic Imidazolium Trihydridoborate and Triphenylborate Species

Molecules ◽  
2020 ◽  
Vol 25 (14) ◽  
pp. 3184
Author(s):  
Maura Pellei ◽  
Riccardo Vallesi ◽  
Luca Bagnarelli ◽  
H. V. Rasika Dias ◽  
Carlo Santini
Keyword(s):  
Mass Spectrometry ◽  
Ionization Mass ◽  
Alkyl Aryl ◽  
X Ray ◽  
X Ray Crystallography ◽  
Microwave Assisted ◽  
Ft Ir ◽  
11B Nmr ◽  
New Compounds ◽  
Ft Ir Spectroscopy

In this study, four new N-(alkyl/aryl)imidazolium-borates were prepared, and their deprotonation reactions were investigated. Addition of BH3•THF to N-benzylimidazoles and N-mesitylimidazoles leads to imidazolium-trihydridoborate adducts. Ammonium tetraphenylborate reacts with benzyl- or mesityl-imidazoles with the loss of one of the phenyl groups yielding the corresponding imidazolium-triphenylborates. Their authenticity was confirmed by CHN analysis, 1H-NMR, 13C-NMR, 11B-NMR, FT-IR spectroscopy, and electrospray ionization mass spectrometry (ESI-MS). 3-Benzyl-imidazolium-1-yl)trihydridoborate, (HImBn)BH3, and (3-mesityl-imidazolium-1-yl)trihydridoborate, (HImMes)BH3, were also characterized by X-ray crystallography. The reactivity of these new compounds as carbene precursors in an effort to obtain borate-NHC complexes was investigated and a new carbene-borate adduct (which dimerizes) was obtained via a microwave-assisted procedure.

scholarly journals Structural isomerism in gold nanoparticles revealed by X-ray crystallography

2015 ◽  
Vol 6 (1) ◽  
Author(s):  
Shubo Tian ◽  
Yi-Zhi Li ◽  
Man-Bo Li ◽  
Jinyun Yuan ◽  
Jinlong Yang ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Single Crystal ◽  
Photoelectron Spectroscopy ◽  
Catalytic Properties ◽  
Ionization Mass ◽  
Important Advance ◽  
Structural Isomers ◽  
X Ray ◽  
X Ray Crystallography ◽  
Structural Isomerism

Abstract Revealing structural isomerism in nanoparticles using single-crystal X-ray crystallography remains a largely unresolved task, although it has been theoretically predicted with some experimental clues. Here we report a pair of structural isomers, Au38T and Au38Q, as evidenced using electrospray ionization mass spectrometry, X-ray photoelectron spectroscopy, thermogravimetric analysis and indisputable single-crystal X-ray crystallography. The two isomers show different optical and catalytic properties, and differences in stability. In addition, the less stable Au38T can be irreversibly transformed to the more stable Au38Q at 50 °C in toluene. This work may represent an important advance in revealing structural isomerism at the nanoscale.

ESI mass spectrometry and X-ray diffraction studies of adducts between anticancer platinum drugs and hen egg white lysozyme

2007 ◽  
pp. 156-158 ◽  
Author(s):  
Angela Casini ◽  
Guido Mastrobuoni ◽  
Claudia Temperini ◽  
Chiara Gabbiani ◽  
Simona Francese ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Egg White ◽  
Platinum Drugs ◽  
Hen Egg White Lysozyme ◽  
X Ray Diffraction ◽  
X Ray ◽  
Egg White Lysozyme ◽  
Esi Mass Spectrometry ◽  
Hen Egg White ◽  
Hen Egg
Sign in / Sign up

Export Citation Format

Share Document