Pankaj Bharmoria

Instituto de Ciencia de Materiales de Sevilla

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Arvind Kumar

Central Salt and Marine Chemicals Research Institute

Kasper Moth‐Poulsen

Institució Catalana de Recerca i Estudis Avançats

Tushar J. Trivedi

Government of the Republic of Korea

Nobuo Kimizuka

Kyushu University

Tejwant Singh Kang

Guru Nanak Dev University

Sónia P. M. Ventura

University of Aveiro

João A. P. Coutinho

University of Aveiro

Nobuhiro Yanai

Japan Science and Technology Agency

Hariom Gupta

Central Institute of Medicinal and Aromatic Plants

Mara G. Freire

University of Aveiro

Cooperative Institutions

Central Salt and Marine Chemicals Research Institute

King Abdulaziz University

Council of Scientific and Industrial Research

University of Aveiro

Aligarh Muslim University

Academy of Scientific and Innovative Research

Bhavnagar University

Kyushu University

Guru Nanak Dev University

University of Gothenburg

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Author Correction: Instantaneous fibrillation of egg white proteome with ionic liquid and macromolecular crowding

Communications Materials (2020)

Pankaj Bharmoria Dibyendu Mondal Matheus M. Pereira Márcia C. Neves Mafalda R. Almeida

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

Proteome

Crowding

White (mutation)

Crowding out

10.1038/s43246-020-00049-3

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Citations (0)

Review: Response to crowded conditions reveals compact nucleus for amyloid formation of folded protein — R0/PR2

Pankaj Bharmoria

Although the consequences of the crowded cell environments may affect protein folding, function and misfolding reactions, these processes are often studied in dilute solutions in vitro. We here used biophysical experiments to investigate the amyloid fibril formation process of the fish protein apo-β-parvalbumin in solvent conditions that mimic steric and solvation aspects of the in vivo milieu. Apo-β-parvalbumin is a folded protein that readily adopts an amyloid state via a nucleation–elongation mechanism. Aggregation experiments in the presence of macromolecular crowding agents (probing excluded volume, entropic effects) as well as small molecule osmolytes (probing solvation, enthalpic effects) revealed that both types of agents accelerate overall amyloid formation, but the elongation step was faster with macromolecular crowding agents but slower in the presence of osmolytes. The observations can be explained by the steric effects of excluded volume favoring assembled states and that amyloid nucleation does not involve monomer unfolding. In contrast, the solvation effects due to osmolyte presence promote nucleation but not elongation. Therefore, the amyloid-competent nuclei must be compact with less osmolytes excluded from the surface than either the folded monomers or amyloid fibers. We conclude that, in contrast to other amyloidogenic folded proteins, amyloid formation of apo-β-parvalbumin is accelerated by crowded cell-like conditions due to a nucleation process that does not involve large-scale protein unfolding.

Osmolyte

Macromolecular Crowding

Amyloid (mycology)

Folding (DSP implementation)

10.1017/qrd.2020.17.pr2

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Recyclable optical bioplastics platform for solid state red light harvesting via triplet–triplet annihilation photon upconversion

Journal of Materials Chemistry A (2022)

Pankaj Bharmoria Fredrik Edhborg Hakan Bildirir Yōichi Sasaki Shima Ghasemi

Sustainable red light harvesting has been achieved in recyclable protein–surfactant–chromophores co-assembled bioplastics with high efficiency due to the efficient diffusion of triplet excited chromophores, and oxygen blockage by protein fibers.

Annihilation

Photon Upconversion

Bioplastic

10.1039/d2ta04810h

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Citations (12)

Structural and Functional Stability of Cellulase in Aqueous-Biamphiphilic Ionic Liquid Surfactant Solution

The Journal of Physical Chemistry B (2014)

Pankaj Bharmoria Mohit J. Mehta Imran Pancha Arvind Kumar

In order to explore the potential of a biamphiphilic ionic liquid surfactant as an enzyme stabilizer in detergents, we have investigated the structural and functional stability of cellulase upon interaction with 3-methyl-1-octylimidazolium dodecylsulfate, [C8mim][C12OSO3], in aqueous medium at pH 4.8. Adsorption and binding isotherms determined from tensiometry and isothermal titration calorimetry indicated that [C8mim][C12OSO3] interacts with cellulase distinctly at the three critical concentrations, viz., aggregation, C1, saturation, C2, and vesicular, C3. Fluorescence (at λex = 280 nm), far UV-circular dichroism spectra, and dynamic light scattering results have shown that [C8mim][C12OSO3] alters the tertiary and secondary structure of cellulase with a slight initial unfolding in the monomeric regime (up to C1), refolding in the aggregation regime (up to C2), and unfolding in the shared aggregation regimes (below C3) and stabilizes the altered conformation in the post-vesicular regime with an overall variation of hydrodynamic diameter from 4.12 to 7.19 nm. A dinitrosalicylic acid sugar assay test showed excellent functional stability of cellulase with an activity of ≥1 unit/mg in all the concentration regimes. A very good surface activity (J. Phys. Chem. B 2012, 116, 14363) complied by the present results vindicates the candidature of [C8mim][C12OSO3] as a potential alternative of mixed micelles or nonionic surfactants for cellulase stabilization in detergent industries.

Isothermal Titration Calorimetry

Hydrophobic effect

10.1021/jp506211b

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Citations (44)

Protein Cohabitation: Improving the Photochemical Stability of R-Phycoerythrin in the Solid State

The Journal of Physical Chemistry Letters (2020)

Pankaj Bharmoria Sandra F. H. Correia Margarida Martins Miguel A. Hernández‐Rodríguez Sónia P. M. Ventura

The poor photochemical stability of R-phycoerythrin (R-PE) has been a bottleneck for its broad-spectrum applications. Inspired by nature, we studied a sustainable strategy of protein cohabitation to enhance R-PE stability by embedding it in a solid matrix of gelatin. Both pure R-PE and fresh phycobiliprotein (PBP) extracts recovered from Gracilaria gracilis were studied. The incorporation of R-PE in the gelatin-based films (gelatin-RPE and gelatin-PBPs) has improved its photochemical stability for at least 8 months, the longest time period reported so far. These results were evidenced by not only absorption but also emission quantum yield measurements (Φ). Moreover, the photostability of gelatin-RPE films upon continuous excitation with an AM1.5G solar simulator was tested and found to remain stable for 23 h after initial decreasing up to 250 min. In the end, another approach was established to allow 100% photostability for a 3 h exposure to an AM1.5G solar simulator by doping the gelatin-based film including R-Phycoerythrin with n-propyl gallate stabilized with Tween 80, allowing their use as naturally based optically active centers in photovoltaic applications.

Gelatin

Phycobiliprotein

Phycoerythrin

10.1021/acs.jpclett.0c01491

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Citations (20)

1-Ethyl-3-methylimidazolium Diethylphosphate Based Extraction of Bioplastic “Polyhydroxyalkanoates” from Bacteria: Green and Sustainable Approach

ACS Sustainable Chemistry & Engineering (2017)

Sonam Dubey Pankaj Bharmoria Praveen Singh Gehlot Vinod Kumar Agrawal Arvind Kumar

An eco-friendly approach toward downstream processing of bacterial biomass for extraction of an intracellular potential bioplastic material polyhydroxyalkanoates replacing chlorinated organic solvents is reported using ionic liquid (IL) 1-ethyl-3-methylimidazolium diethylphosphate ([C2mim][(C2)2OPO3]) as an extractant. [C2mim][(C2)2OPO3] dissolved wet bacterial biomass of Halomonas hydrothermalis (MTCC accession no. 5445; NCBI Genbank accession no. GU938192), with ease on account of its high hydrogen bond basicity (β = 1.07). The recovered polymer with a yield of 60% ± 2% was characterized using 1H NMR, FT-IR, and TGA techniques and confirmed to be polyhydroxybutyrate (PHB). The properties of PHB were found to be in close proximity to the standard PHB. The [C2mim][(C2)2OPO3] was recovered with 60% yield and retention of chemical structure after two consecutive dissolution cycles, which minimized the cost of developed process. The recovered PHB was used to prepare a bioplastic film, which showed good thermal and mechanical stability, as characterized by FT-IR, DSC, TGA, and DMA techniques.

Bioplastic

Polyhydroxybutyrate

Phosphonium

10.1021/acssuschemeng.7b03096

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Citations (59)

Protein cohabitation: long-term immunoglobulin G storage at room temperature

Journal of Materials Chemistry B (2023)

Pankaj Bharmoria Saik Ann Ooi Andrea Cellini Daniel Tietze Michał Maj

We report a simple bioinspired strategy of protein cohabitation for long-term functional storage of therapeutic proteins at room temperature.

Gelatin

10.1039/d3tb00161j

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Simple and Versatile Platform for Air-Tolerant Photon Upconverting Hydrogels by Biopolymer–Surfactant–Chromophore Co-assembly

Journal of the American Chemical Society (2018)

Pankaj Bharmoria Shota Hisamitsu Hisanori Nagatomi Taku Ogawa Masa‐aki Morikawa

Exploration of triplet–triplet annihilation based photon upconversion (TTA-UC) in aqueous environments faces difficulty such as chromophores insolubility and deactivation of excited triplets by dissolved oxygen molecules. We propose a new strategy of biopolymer–surfactant–chromophore coassembly to overcome these issues. Air-stable TTA-UC with a high upconversion efficiency of 13.5% was achieved in hydrogel coassembled from gelatin, Triton X-100 and upconverting chromophores (triplet sensitizer and emitter). This is comparable to the highest UC efficiency observed to date for air-saturated aqueous UC systems. Moreover, this is the first example of air-stable TTA-UC in the form of hydrogels, widening the applicability of TTA-UC in biological applications. The keys are two-fold. First, gelatin and the surfactant self-assemble in water to give a developed hierarchical structure with hydrophobic domains which accommodate chromophores up to high concentrations. Second, thick hydrogen-bonding networks of gelatin backbone prevent O2 inflow to the hydrophobic interior, as evidenced by long acceptor triplet lifetime of 4.9 ms. Air-stable TTA-UC was also achieved for gelatin with other nonionic surfactants (Tween 80 and Pluronic f127) and Triton X-100 with other gelling biopolymers (sodium alginate and agarose), demonstrating the versatility of current strategy.

Chromophore

Biopolymer

Gelatin

Photon Upconversion

10.1021/jacs.8b05821

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Citations (78)

Effect of cationic head group on micellization behavior of new amide-functionalized surface active ionic liquids

Physical Chemistry Chemical Physics (2014)

Raman Kamboj Pankaj Bharmoria Vinay Chauhan Gurbir Singh Arvind Kumar

The functionalization of the alkyl chain with an amide group led to marked changes in the characteristic properties of micellization of different SAILs.

Cationic polymerization

Amide

10.1039/c4cp04054f

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Citations (62)

Triplet-Triplet Annihilation Mediated Photon Upconversion Solar Energy Systems

Materials Chemistry Frontiers (2023)

Lukas Naimovičius Pankaj Bharmoria Kasper Moth‐Poulsen

Triplet–triplet annihilation mediated solar energy harvesting systems for a global transition toward carbon-neutral energy technologies.

Annihilation

Photon Upconversion

10.1039/d3qm00069a

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Citations (32)