scholarly journals Unusual Structural Features in the Adduct of Dirhodium Tetraacetate with Lysozyme

2021 ◽  
Vol 22 (3) ◽  
pp. 1496
Author(s):  
Domenico Loreto ◽  
Giarita Ferraro ◽  
Antonello Merlino
Keyword(s):  
Anticancer Agents ◽  
Structural Features ◽  
Side Chain ◽  
Side Chains ◽  
Valuable Insight ◽  
Experimental Conditions ◽  
Egg White Lysozyme ◽  
Potential Applications ◽  
Model Protein ◽  
Hen Egg White

The structures of the adducts formed upon reaction of the cytotoxic paddlewheel dirhodium complex [Rh2(μ-O2CCH3)4] with the model protein hen egg white lysozyme (HEWL) under different experimental conditions are reported. Results indicate that [Rh2(μ-O2CCH3)4] extensively reacts with HEWL:it in part breaks down, at variance with what happens in reactions with other proteins. A Rh center coordinates the side chains of Arg14 and His15. Dimeric Rh–Rh units with Rh–Rh distances between 2.3 and 2.5 Å are bound to the side chains of Asp18, Asp101, Asn93, and Lys96, while a dirhodium unit with a Rh–Rh distance of 3.2–3.4 Å binds the C-terminal carboxylate and the side chain of Lys13 at the interface between two symmetry-related molecules. An additional monometallic fragment binds the side chain of Lys33. These data, which are supported by replicated structural determinations, shed light on the reactivity of dirhodium tetracarboxylates with proteins, providing useful information for the design of new Rh-containing biomaterials with an array of potential applications in the field of catalysis or of medicinal chemistry and valuable insight into the mechanism of action of these potential anticancer agents.

Oxaliplatin vs. cisplatin: competition experiments on their binding to lysozyme

2015 ◽  
Vol 44 (22) ◽  
pp. 10392-10398 ◽  
Author(s):  
Daniela Marasco ◽  
Luigi Messori ◽  
Tiziano Marzo ◽  
Antonello Merlino
Keyword(s):  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Model Protein ◽  
Hen Egg White ◽  
Hen Egg

The model protein hen egg white lysozyme was challenged with oxaliplatin and cisplatin.

Comparative study of dG affinity vs. DNA methylation modulating properties of side chain derivatives of procainamide: insight into its DNA hypomethylating effect

RSC Advances ◽  
2016 ◽  
Vol 6 (7) ◽  
pp. 5350-5358 ◽  
Author(s):  
R. L. Gawade ◽  
D. K. Chakravarty ◽  
J. Debgupta ◽  
E. Sangtani ◽  
S. Narwade ◽  
...  
Keyword(s):  
Dna Methylation ◽  
Comparative Study ◽  
Structural Features ◽  
Side Chain ◽  
Side Chains ◽  
Hypomethylating Agents ◽  
Derivatives Of ◽  
Insight Into

Structural features of side-chains govern the association of procainamide and its derivatives with dG base of CpG rich DNA, which may differentially hinder the activity of DNMT-1, thereby they act as DNA hypomethylating agents.

scholarly journals In Vitro, D-Ribose and Formaldehyde Glycating Effects on Hen Egg White Lysozyme

2021 ◽  
Keyword(s):  
Cell Damage ◽  
Egg White ◽  
Cross Linking ◽  
Hen Egg White Lysozyme ◽  
Time Duration ◽  
Experimental Conditions ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hen Egg

Background: Glycation causes severe damage to the protein structure, instigating different diseases like cataracts, nephropathy, vasculopathy, retinopathy, atherosclerosis, neurodegenerative disease, diabetes, and age-dependent complications. Formaldehyde, a pollutant present in human habitation, is produced endogenously or exogenously during cooking or incinerating wood, paints, furniture, chipboards, fabric etc. Its higher concentrations can cause cell damage that promotes the formation of DNA/Protein cross-links. The present study aimed to evaluate the glycating effects of formaldehyde on hen egg white lysozyme in comparison with known glycating agent D-ribose. Methods: In this, in-vitro study, hen egg white lysozyme (HEWL) glycation with different concentrations of formaldehyde (0.25mM, 0.5mM, 1mM and 2mM) and D-ribose (0.01mM, 0.05mM, 0.1mM and 0.5mM) was examined using two different experimental conditions: concentration and time duration. Further cross-linking of protein was also analysed using SDS-PAGE technique. Results: Glycation of HEWL treated with formaldehyde increased with increasing concentrations (0.25mM, 0.5mM, 1mM and 2mM) and time duration (1, 3, 7 and 15 days). Cross linking of HEWL showed visible glycation at 2mM concentration. Cross-linked HEWL products gave dimer at 0.25mM and 0.5mM and trimers at 1mM and 2mMat 3, 7 and 15days. However, compared to formaldehyde, D-ribose glycation at different concentrations (0.01mM, 0.05mM, 0.1mM and 0.5mM) did not show the prominent cross linking of protein. Conclusion: Formaldehyde was found to be a more potent glycating agent compared to D-ribose. Compared to D-ribose, formaldehyde can produce protein misfolding and can be used in clinical research to establish the role of formaldehyde in patients with diseases.

scholarly journals Structural Features Defining NF-κB Inhibition by Lignan-Inspired Benzofurans and Benzothiophenes

Biomolecules ◽  
2020 ◽  
Vol 10 (8) ◽  
pp. 1131
Author(s):  
Toan Dao-Huy ◽  
Simone Latkolik ◽  
Julia Bräuer ◽  
Andreas Pfeil ◽  
Hermann Stuppner ◽  
...  
Keyword(s):  
Significant Influence ◽  
Inhibitory Activity ◽  
Structure Activity Relationship ◽  
Structural Features ◽  
Activity Relationship ◽  
Side Chain ◽  
Side Chains ◽  
Substitution Pattern ◽  
Structure Activity

A series of 2-arylbenzofurans and 2-arylbenzothiophenes was synthesized carrying three different side chains in position five. The synthesized compounds were tested for NF-κB inhibition to establish a structure activity relationship. It was found that both, the side chain in position five and the substitution pattern of the aryl moiety in position two have a significant influence on the inhibitory activity.

Structural Determinants of Protein Dynamics: Analysis of 15N NMR Relaxation Measurements for Main-Chain and Side-Chain Nuclei of Hen Egg White Lysozyme

Biochemistry ◽  
1995 ◽  
Vol 34 (12) ◽  
pp. 4041-4055 ◽  
Author(s):  
Matthias Buck ◽  
Jonathan Boyd ◽  
Christina Redfield ◽  
Donald A. MacKenzie ◽  
David J. Jeenes ◽  
...  
Keyword(s):  
Main Chain ◽  
Nmr Relaxation ◽  
Side Chain ◽  
15N Nmr ◽  
Hen Egg White Lysozyme ◽  
Structural Determinants ◽  
Egg White Lysozyme ◽  
15N Nmr Relaxation ◽  
Relaxation Measurements ◽  
Hen Egg White

scholarly journals Peptide/Peptoid Hybrid Oligomers: The Influence of Hydrophobicity and Relative Side-Chain Length on Antibacterial Activity and Cell Selectivity

Molecules ◽  
2019 ◽  
Vol 24 (24) ◽  
pp. 4429 ◽  
Author(s):  
Nicki Frederiksen ◽  
Paul R. Hansen ◽  
Fredrik Björkling ◽  
Henrik Franzyk
Keyword(s):  
Antibacterial Activity ◽  
Chain Length ◽  
Hydrophobic Surface ◽  
Structural Features ◽  
Side Chain ◽  
Side Chains ◽  
Side Chain Length ◽  
E Coli ◽  
Cell Selectivity ◽  
Wide Range

Previous optimisation studies of peptide/peptoid hybrids typically comprise comparison of structurally related analogues displaying different oligomer length and diverse side chains. The present work concerns a systematically constructed series of 16 closely related 12-mer oligomers with an alternating cationic/hydrophobic design, representing a wide range of hydrophobicity and differences in relative side-chain lengths. The aim was to explore and rationalise the structure–activity relationships within a subclass of oligomers displaying variation of three structural features: (i) cationic side-chain length, (ii) hydrophobic side-chain length, and (iii) type of residue that is of a flexible peptoid nature. Increased side-chain length of cationic residues led to reduced hydrophobicity till the side chains became more extended than the aromatic/hydrophobic side chains, at which point hydrophobicity increased slightly. Evaluation of antibacterial activity revealed that analogues with lowest hydrophobicity exhibited reduced activity against E. coli, while oligomers with the shortest cationic side chains were most potent against P. aeruginosa. Thus, membrane-disruptive interaction with P. aeruginosa appears to be promoted by a hydrophobic surface of the oligomers (comprised of the aromatic groups shielding the cationic side chains). Peptidomimetics with short cationic side chains exhibit increased hemolytic properties as well as give rise to decreased HepG2 (hepatoblastoma G2 cell line) cell viability. An optimal hydrophobicity window could be defined by a threshold of minimal hydrophobicity conferring activity toward E. coli and a threshold for maximal hydrophobicity, beyond which cell selectivity was lost.

scholarly journals Chemical conversion of cisplatin and carboplatin with histidine in a model protein crystallized under sodium iodide conditions

2014 ◽  
Vol 70 (9) ◽  
pp. 1127-1131 ◽  
Author(s):  
Simon W. M. Tanley ◽  
John R. Helliwell
Keyword(s):  
Anticancer Agents ◽  
Sodium Iodide ◽  
Chloride Concentration ◽  
Chemical Conversion ◽  
Monoclinic Space Group ◽  
Asymmetric Unit ◽  
High Sodium ◽  
Egg White Lysozyme ◽  
Model Protein ◽  
Partial Chemical

Cisplatin and carboplatin are platinum anticancer agents that are used to treat a variety of cancers. Previous X-ray crystallographic studies of carboplatin binding to histidine in hen egg-white lysozyme (HEWL) showed a partial chemical conversion of carboplatin to cisplatin owing to the high sodium chloride concentration used in the crystallization conditions. Also, the co-crystallization of HEWL with carboplatin in sodium bromide conditions resulted in the partial conversion of carboplatin to the transbromoplatin form, with a portion of the cyclobutanedicarboxylate (CBDC) moiety still present. The results of the co-crystallization of HEWL with cisplatin or carboplatin in sodium iodide conditions are now reported in order to determine whether the cisplatin and carboplatin converted to the iodo form, and whether this took place in a similar way to the partial conversion of carboplatin to cisplatin in NaCl conditions or to transbromoplatin in NaBr conditions as seen previously. It is reported here that a partial chemical transformation has taken place to a transplatin form for both ligands. The NaI-grown crystals belonged to the monoclinic space groupP21with two molecules in the asymmetric unit. The chemically transformed cisplatin and carboplatin bind to both His15 residues,i.e.in each asymmetric unit. The binding is only at the Nδatom of His15. A third platinum species is also seen in both conditions bound in a crevice between symmetry-related molecules. Here, the platinum is bound to three I atoms identified based on their anomalous difference electron densities and their refined occupancies, with the fourth bound atom being a Cl atom (in the cisplatin case) or a portion of the CBDC moiety (in the carboplatin case).

Methylation at lysine side chain of hen egg white lysozyme (HEWL) promote its amyloid formation

2011 ◽  
Vol 44 (13) ◽  
pp. S23-S24
Author(s):  
Ostadi Hassan ◽  
Shariat Sajjad ◽  
Ali Akbar Meratan ◽  
Ali Es-haghi ◽  
Mohsen Nemat-Gorgani
Keyword(s):  
Egg White ◽  
Side Chain ◽  
Amyloid Formation ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Lysine Side Chain ◽  
Hen Egg White ◽  
Hen Egg
Sign in / Sign up

Export Citation Format

Share Document