Cytochrom‐<i>c</i>‐Calixaren‐Kristalle auf Elektroden: intermolekularer Elektronentransfer zwischen definiert lokalisierten Redoxzentren

McGovern, Róise E.; Feifel, Sven C.; Lisdat, Fred; Crowley, Peter B.

doi:10.1002/ange.201500191

Cited by 9 publications

(3 citation statements)

References 26 publications

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“…[4,5] More recently, they have also been proposed as additives for protein co-crystallization, not only for their nucleating properties [6] but also because of the phasing ability of the lanthanide center for X-ray crystallography. [7][8][9] In addition, lanthanide complexes can act as "molecular glues" [10][11][12] , which can contribute to consolidate protein-protein interfaces. However, the precise mechanism of the interaction between lanthanide complexes and biomolecules in solution remains unclear, hence the need to develop a comprehensive understanding of the dynamic process of non-covalent binding.…”

Section: Introductionmentioning

confidence: 99%

One Touch Is All It Takes: the Supramolecular Interaction between Ubiquitin and Lanthanide Complexes Revisited by Paramagnetic NMR and Molecular Dynamics

Dos Santos,

Bartocci,

Gillet

et al. 2024

Preprint

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The supramolecular interaction between lanthanide complexes and proteins is at the heart of numerous chemical and biological studies. Some of these complexes have demonstrated remarkable interaction properties with proteins or peptides in solution and in the crystalline state. Here we have used the paramagnetism of lanthanide ions to characterize the affinity of two lanthanide complexes for ubiquitin. As the interaction process is dynamic, the acquired NMR data only reflect the time average of the different steps. We have used molecular dynamics (MD) simulations to get a deeper insight into the detailed interaction scenario at the microsecond scale. This NMR/MD approach enabled us to establish that the tris-dipicolinate complex interacts specifically with arginines and lysines, while the crystallophore explores the protein surface through weak interactions with carboxylates. These observations shed new light on the dynamic interaction properties of these complexes, which will ultimately enable us to propose a crystallization mechanism.

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Section: Introductionmentioning

confidence: 99%

One Touch Is All It Takes: the Supramolecular Interaction between Ubiquitin and Lanthanide Complexes Revisited by Paramagnetic NMR and Molecular Dynamics

Dos Santos,

Bartocci,

Gillet

et al. 2024

Preprint

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“…18,19 The use of SAMs has also been reported to support the assembly of microscale crystals of redox proteins for constructing bioelectronic devices. 20 Also, alternative approaches to foreign surfaces have been reported to promote crystallization. For example, the rational engineering of a protein surface to reduce the conformational entropy has been proposed.…”

Section: Introductionmentioning

confidence: 99%

Self-Assembled Monolayers As a Tool to Investigate the Effect of Surface Chemistry on Protein Nucleation

Artusio

Gavira

Pisano

2023

Crystal Growth & Design

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Modified surfaces like siliconized glass are commonly used to support protein crystallization and facilitate obtaining crystals. Over the years, various surfaces have been proposed to decrease the energetic penalty required for consistent protein clustering, but scarce attention has been paid to the underlying mechanisms of interactions. Here, we propose self-assembled monolayers that are surfaces exposing fine-tuned moieties with a very regular topography and subnanometer roughness, as a tool to unveil the interaction between proteins and functionalized surfaces. We studied the crystallization of three model proteins having progressively narrower metastable zones, i.e., lysozyme, catalase, and proteinase K, on monolayers exposing thiol, methacrylate, and glycidyloxy groups. Thanks to comparable surface wettability, the induction or the inhibition of nucleation was readily attributed to the surface chemistry. For example, thiol groups strongly induced the nucleation of lysozyme thanks to electrostatic pairing, whereas methacrylate and glycidyloxy groups had an effect comparable to unfunctionalized glass. Overall, the action of surfaces led to differences in nucleation kinetics, crystal habit, and even crystal form. This approach can support the fundamental understanding of the interaction between protein macromolecules and specific chemical groups, which is crucial for many technological applications in the pharmaceutical and food industry.

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“…Once one crystallization condition for a protein has been discovered, few researchers search for different conditions unless they are guaranteed to provide new biological information such as ligand-binding information, structural differences at various pH values or complex structures with other proteins. However, exploring different crystallization conditions is important to establish a guideline for the rational design of protein molecular packings, because protein crystals have been regarded as novel practical frameworks for biomolecular devices (Abe & Ueno, 2015;McGovern et al, 2015). One of the model proteins for protein crystal engineering is the blue copper protein, which functions in electron-transport chains and contains a mononuclear copper (Cu) centre that is usually coordinated by two histidine (His) residues, one cysteine (Cys) residue and one methionine (Met) residue.…”

Section: Introductionmentioning

confidence: 99%

New molecular packing in a crystal of pseudoazurin fromAlcaligenes faecalis: a double-helical arrangement of blue copper

2017

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Pseudoazurin from the denitrifying bacterium Alcaligenes faecalis (AfPAz) is a blue copper protein and functions as an electron donor to copper-containing nitrite reductase (CuNIR). Conventionally, AfPAz has been crystallized using highly concentrated ammonium sulfate as a precipitant. Here, a needle-like crystal of AfPAz grown in a solution containing a macromolecular precipitant, polyethylene glycol 8000 (PEG 8000), is reported. The crystal belonged to space group P6, with unit-cell parameters a = b = 68.7, c = 94.2 Å. The structure has been determined and refined at 2.6 Å resolution. The asymmetric unit contained two AfPAz molecules contacting each other on negatively charged surfaces. The molecular packing of the crystal showed a right-handed double-helical arrangement of AfPAz molecules and hence of blue copper sites. This structure provides insight into the excluded-volume effect of PEG and the manner of assembly of AfPAz.

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Cytochrom‐c‐Calixaren‐Kristalle auf Elektroden: intermolekularer Elektronentransfer zwischen definiert lokalisierten Redoxzentren

Cited by 9 publications

References 26 publications

One Touch Is All It Takes: the Supramolecular Interaction between Ubiquitin and Lanthanide Complexes Revisited by Paramagnetic NMR and Molecular Dynamics

One Touch Is All It Takes: the Supramolecular Interaction between Ubiquitin and Lanthanide Complexes Revisited by Paramagnetic NMR and Molecular Dynamics

Self-Assembled Monolayers As a Tool to Investigate the Effect of Surface Chemistry on Protein Nucleation

New molecular packing in a crystal of pseudoazurin fromAlcaligenes faecalis: a double-helical arrangement of blue copper

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