Co-assembly-mediated biosupramolecular catalysis: thermodynamic insights into nucleobase specific (oligo)nucleotide attachment and cleavage

Priyanka,; Maiti, Subhabrata

doi:10.1039/d3tb01747h

J. Mater. Chem. B

2023

DOI: 10.1039/d3tb01747h

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Co-assembly-mediated biosupramolecular catalysis: thermodynamic insights into nucleobase specific (oligo)nucleotide attachment and cleavage

Priyanka,

Subhabrata Maiti

Abstract: A co-assembly-mediated biosupramolecular oligonucleotide digestion process is reported, comprising Zn(ii)-metallosurfactant and alkaline phosphatase, which gets accelerated or decelerated depending on the type of nucleobases.

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2024

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Cited by 3 publications

References 75 publications

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Salt Gradient-Induced Phoresis of Vesicles and Enhanced Membrane Fusion in a Crowded Milieu

Yadav,

Sivoria,

Maiti

2024

J. Phys. Chem. B

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Phoresis of biocolloidal objects in response to chemical gradients is a matter of interest among diverse scientific disciplines owing to their importance in the spatiotemporal orchestration of biochemical processes. Although there are reports of soft matter transport/phoresis in the gradient of ions or salts in the aqueous system, their phoretic behavior in the presence of macromolecular crowder is largely unexplored. Notably, cellular cytoplasm is illustrated as a crowded milieu and thereby understanding biomolecular phoresis in the presence of polymeric macromolecules would endorse phoretic behavior in a biomimetic environment. Here, we report the phoresis-induced enhanced aggregation and fusion of vesicles in gradients of monovalent (NaCl) and divalent salt (MgCl 2 ), in the presence of polymeric crowder, polyethylene glycol of molecular weight 400 (PEG 400). Apart from diffusiophoresis, depletion force plays a crucial factor in crowded environments to control localized vesicle aggregation in a salt gradient. This demonstration will potentially show the pathway to future research related to spatiotemporally correlated liposomal transport and membrane-dependent function (such as content mixing and signaling) in a physiologically relevant crowded environment.

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Salt Gradient-Induced Phoresis of Vesicles and Enhanced Membrane Fusion in a Crowded Milieu

Yadav,

Sivoria,

Maiti

2024

J. Phys. Chem. B

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Probing Phoretic Transport of Oxidative Enzyme-Bound Zn(II)-Metallomicelle in Adenosine Triphosphate Gradient via a Spatially Relocated Biocatalytic Zone

Priyanka,

Maiti

2024

Langmuir

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Nucleotide-mediated modulation of chemoselective protein functionalization in a liquid-like condensed phase

Ettikkan,

Priyanka,

Mahato

et al. 2024

Commun Chem

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Liquid-like protein condensates are ubiquitous in cellular system and are increasingly recognized for their roles in physiological processes. Condensed phase harbors distinctive chemical microenvironment, markedly different than dilute aqueous phase. Herein, we demonstrate chemoselective modification pattern of nucleophilic canonical amino acid sidechains (namely – cysteine, tyrosine and lysine) of the protein towards 4-chloro-7-nitrobenzofurazan in the dilute and condensed phase. We also delineate how the effect of nucleotides and their in situ enzymatic dissociation temporally modulate the protein condensate’s pH and the protein’s corresponding chemoselective modification. We have shown that the pH of the condensate decreases in the presence of nucleoside triphosphate, whereas it increases in the presence of nucleoside monophosphates or phosphate ion. For instance, we find lysine-specific modification gets inhibited in the presence of adenosine triphosphate (ATP), but significantly enhanced in the presence of monophosphates. This feature enables us to gain temporal control over dynamic change in protein functionalization via enzymatic ATP hydrolysis. Overall, this work substantiates the alteration in pH-responsiveness of Brønsted basicity of a protein’s ε-amine in the condensed phase. Furthermore, this environment sensitivity in chemoselective protein functionalization in condensed phase will be important in adaptable protein engineering to the chemical biology of protein phase separation.

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Co-assembly-mediated biosupramolecular catalysis: thermodynamic insights into nucleobase specific (oligo)nucleotide attachment and cleavage

Abstract: A co-assembly-mediated biosupramolecular oligonucleotide digestion process is reported, comprising Zn(ii)-metallosurfactant and alkaline phosphatase, which gets accelerated or decelerated depending on the type of nucleobases.

Cited by 3 publications

References 75 publications

Salt Gradient-Induced Phoresis of Vesicles and Enhanced Membrane Fusion in a Crowded Milieu

Salt Gradient-Induced Phoresis of Vesicles and Enhanced Membrane Fusion in a Crowded Milieu

Probing Phoretic Transport of Oxidative Enzyme-Bound Zn(II)-Metallomicelle in Adenosine Triphosphate Gradient via a Spatially Relocated Biocatalytic Zone

Nucleotide-mediated modulation of chemoselective protein functionalization in a liquid-like condensed phase

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