Spectroscopy, Biophysics, Physical and Theoretical Chemistry, Catalysis
127
Scopus Publications
4069
Scholar Citations
35
Scholar h-index
87
Scholar i10-index
Scopus Publications
Switchable pathways for precise carboxylic acid modification in proteins and antibodies Rajib Molla, Rohith Singudas, Dwaipayan Biswas, Lucky Ojha, Divya Bindra, Saurabh Rai, V. Ragendu, Saptarshi Mukherjee, Ram Kumar Mishra, Vishal Rai Cell Reports Physical Science, 2026 Historically, organic chemistry has been biased toward irreversible transformations. However, they have struggled to meet the selectivity demands from recent biopharma growth. Here, we establish the potential of reversible reactions within a multi-equilibria system from a multicomponent reaction (MCR), offering three switchable pathways for selective carboxylate modification in proteins and antibodies. The classical Ugi reaction yields heterogeneous mixtures, lysine being a major competitor. To address this, we developed a four-component reaction to render a four-component product (4CR-4CP). The 4CR-4CP can be disrupted and switched to 4CR-2CP or 3CR-2CP (>36 examples). Pathway exclusivity and carboxylate selectivity remain intact even at >99% bioconjugation. The method enables single- or dual-site probe installation and E21-labeling of insulin without compromising receptor binding or downstream signaling. The strategy extends to monoclonal antibodies, generating carboxylate-selective antibody-fluorophore and drug conjugates (AFCs and ADCs) for antigen-specific labeling and antiproliferative activity, opening a unique platform for multi-equilibria driven protein modification.
Association Interactions of Hydroxychloroquine Sulfate With DMPG Liposomes: CTAB-Induced Lipid Solubilization and Subsequent Drug Release Rahul Yadav, Subhasis Das, Debanggana Shil, Saptarshi Mukherjee Chemistry an Asian Journal, 2026 Herein, we investigated the molecular interactions of an antimalarial drug, hydroxychloroquine sulfate (HCQS), with liposome nanocarriers. Spectroscopic analyses revealed that in the presence of the anionic liposomes (DMPG), HCQS undergoes significant microenvironmental changes, including a marginal red shift in absorption, a 17 nm blue shift in emission, and a marked reduction in fluorescence lifetime, indicating a partial localization of the drug within the liposomal hydrophobic bilayer. Steady‐state and time‐resolved anisotropy measurements revealed the restricted probe mobility in liposomal environments. However, cholesterol‐dependent studies indicated that increased membrane rigidity reduced the HCQS‐liposome association interactions. Furthermore, solubilization of the anionic liposomes by a cationic surfactant, CTAB led to the complete release of the bound HCQS, with reversibility in spectral signatures. It is suggested that due to mixed micelle formation between CTAB and the lipid molecules, the drug gets released from the liposome environment. These findings highlight the interplay of electrostatic and hydrophobic forces in governing the HCQS–liposome association and provide valuable insights for rational design of liposome‐based drug delivery systems.
Esterase-like “Superactivity” of Apo-Human Serum Transferrin: Specific Role of Hydrophobic Tail Chain Length and Charge of Headgroup of Surfactants Rahul Yadav, Subhasis Das, Sadrish Ghosh, Debanggana Shil, Arghajit Pyne, Saptarshi Mukherjee Biochemistry, 2026 High Resolution Image Download MS PowerPoint Slide The enhanced catalytic activity (superactivity) of iron-depleted apo-human serum transferrin (apo-hTF) in the presence of cationic surfactants with varying chain lengths has been investigated in this work. The progress of ester hydrolysis of two different esterase substrates, para- nitrophenylacetate (PNPA) and 4-methylumbelliferylacetate (4-MUA), was monitored spectroscopically. Catalytic activity of apo-hTF gets enhanced with increasing concentrations of cationic surfactants, up to the micellar concentration, followed by a gradual decrease at postmicellar concentrations. However, the catalytic performance of the protein remained silent in its native form, in the presence of anionic and neutral surfactants, guanidinium hydrochloride-denatured conformation, temperature-induced aggregated form, and liquid–liquid phase-separated (LLPS) form of the protein. This work sheds light on the importance of the location and alignment of amino acids in the catalytic hub and the approachability of the substrate at the active site in micellar catalysis systems. These results provide new insights into enzyme–substrate interactions in the domain of micellar catalysis, potentially aiding the design of surfactant-based catalytic systems.
Effect of Water–DMSO Binary Solvent Mixture on the Behavior of an Intrinsically Disordered Protein, β-Casein Saurabh Rai, Debanggana Shil, Bijan Kumar Paul, Saptarshi Mukherjee Journal of Physical Chemistry B, 2025 The study of protein behavior in water-dimethyl sulfoxide (DMSO) solvent mixture is of great interest in biophysical research, as DMSO is a widely used cosolvent in various experimental assays. However, investigating the behavior of intrinsically disordered proteins (IDPs) in a water-DMSO binary solvent mixture is still in its infancy. Herein, we present a comprehensive analysis of the behavior of β-casein (βCN), an IDP, in water-DMSO mixtures using a combination of steady-state fluorescence, time-resolved anisotropy, infrared spectroscopy, and fluorescence correlation spectroscopy (FCS), characterizing the protein stability and conformational dynamics. FCS analysis with Alexa-488-labeled βCN, revealed the variations in hydrodynamic radius with varying content of DMSO, signifying constrained mobility and expanded size of the protein. Further, fluorescence self-quenching of the fluorophore (Alexa-488) was analyzed to probe the conformational dynamics of βCN, with changes in the time constant suggesting protein unfolding followed by an assembly at higher DMSO content. These results were corroborated by infrared spectroscopy, where an increase in the amide-I absorption band indicated the formation of intermolecular antiparallel β-sheet aggregates. At higher DMSO concentrations, additional structural features were observed, which were further examined using optical and field emission scanning electron microscopy (FESEM).
Impact of Intrinsic Hydrophobicity of Bile Salts on the Inhibition of Temperature-Induced Aggregation of Bovine Serum Albumin Rahul Yadav, Atanu Nandy, Dwaipayan Biswas, Saptarshi Mukherjee Chemphyschem, 2025 Bile salts are highly hydrophobic biosurfactants known for their unconventional structure and abnormal micellization properties, which aid in several biological processes. The intrinsic hydrophobicity of bile salts plays a pivotal role during the binding interactions of these molecules with other biomolecules. The inhibition effects of three bile salts, sodium taurocholate (NaTC), sodium cholate (NaC), and sodium deoxycholate (NaDC), on the temperature‐induced aggregation of BSA are explored. The results acquired from the Thioflavin T (ThT) assay and circular dichroism (CD) experiments demonstrate that all three bile salts can inhibit the BSA aggregation. Additionally, NaDC can have a prominent aggregation inhibition propensity for BSA compared to the other two bile salts. The inhibitory action of three bile salts toward BSA aggregation followed a particular order, complementing their intrinsic hydrophobicity. Further, binding interactions of native BSA with bile salts are characterized by tryptophan fluorescence emission, fluorescence lifetime studies, site marker studies, isothermal titration calorimetry, and thermal melting experiments. The results of these studies substantiate that bile salts bind to the native protein through strong hydrophobic forces and provide significant stabilization to the native conformation of the protein, which subsequently impedes the protein from aggregating.
Intracellular Subdegree Temperature Sensing and Dynamics by Thermoresponsive Silver Nanoclusters as Molecular Probes Saurabh Rai, Sameeksha Agrawal, Saptarshi Mukherjee Journal of Physical Chemistry Letters, 2025 High Resolution Image Download MS PowerPoint Slide Reported herein are long-lived, red-luminescent silver nanoclusters (AgNCs) protected by the small-molecule ligand thiolactic acid, which exhibit exceptional stability (shelf life exceeding three years, photostability ∼100%), water-solubility, and high biocompatibility, making them suitable for diverse applications such as sensing and live-cell imaging. The AgNCs display extremely sensitive (>2% K –1 ) temperature-dependent luminescence, monitored by a dual approach of changes in photoluminescence intensity and excited-state lifetime, enabling precise local thermal environment monitoring with a very high-resolution temperature sensing down to subdegree levels (<0.5 K). MTT assay, confocal fluorescence imaging, and fluorescence lifetime imaging microscopy (FLIM) analysis of mammalian cells suggest that the non-cytotoxic AgNCs specifically stain lysosomes in live cells, functioning as an organelle-specific biomarker and providing critical insights into lysosomal dynamics and intracellular temperature fluctuations. The unique properties of these AgNCs, corroborated by detailed mechanistic studies, open new avenues for studying nanoscale subcellular physiology and developing temperature-sensitive diagnostics and preservation strategies.
Modulating the spectroscopic signatures of gold nanoclusters: The role of hydrophobicity of bile salts Niranjan Mohite, Khokan Paria, Paritosh Mahato, Saptarshi Mukherjee Journal of Surfactants and Detergents, 2025 Deciphering the role of hydrophobicity of the capping ligands on the development of luminescent Metal Nanoclusters (MNCs) is a longstanding endeavor and demands more comprehensive scientific investigations. Hence, our attempts have been directed to explore this scarcely reported fact by adopting the rather non‐conventional top‐down approach for the development of MNCs. Herein, we are reporting the synthesis of the highly stable Cysteamine‐templated gold nanoclusters (AuNCs) with different photophysical properties from the core etching of bile salts‐templated Metal Nanoparticles (MNPs). Herein, we have used three different bile salts (sodium cholate, NaC; sodium taurocholate, NaTC; and sodium deoxycholate, NaDC) with varying hydrophobicity index. The role of hydrophobicity of the bile salts (NaDC > NaC > NaTC) had a profound influence on the synthesis of the AuNPs, as well as in the synthesis of AuNCs by the core etching of different AuNPs. It was observed that the core etching of these three AuNPs, templated by NaC (NP1), NaDC (NP2), and NaTC (NP3) with a common etching agent cysteamine, leads to the formation of three AuNCs (Cystm@AuNC1 derived from NP1, Cystm@AuNC2 derived from NP2, and Cystm@AuNC3 derived from NP3) characterized by different photophysical signatures.
Successive ferroelectric orders and magnetoelectric coupling without long-range magnetic order in highly frustrated pyrochlore compounds: Sm2Ti2−xVxO7 S. Mukherjee, A. Pal, F. Tuzi, A. Polimeni, T. W. Yen, O. Ivashko, S. Majumdar, A. Kumar, S. Giri Physical Review B, 2025 ${\mathrm{Sm}}_{2}{\mathrm{Ti}}_{2}{\mathrm{O}}_{7}$, a member of the rare-earth titanate pyrochlores, exhibits dipolar-octupolar antiferromagnetism below ${T}_{N}=0.35\phantom{\rule{4pt}{0ex}}\mathrm{K}$. We observed two ferroelectric transitions at 182 (${T}_{\text{FE}1}$) and 52 K (${T}_{\text{FE}2}$), significantly higher than ${T}_{N}$ for ${\mathrm{Sm}}_{2}{\mathrm{Ti}}_{2\ensuremath{-}x}{\mathrm{V}}_{x}{\mathrm{O}}_{7}$ ($x=0,0.1$). Although the ferroelectric transition temperatures remain unchanged, the polarization value decreases with V doping. A structural transition to a polar $R3m$ rhombohedral phase from the cubic $Fd\overline{3}m$ structure occurs at ${T}_{\text{FE}1}$ for the pristine compound, involving a distortion in the pyrochlore lattices formed by the Sm atoms. Remarkably, linear magnetoelectric coupling is observed in both compounds, with further enhancement of magnetoelectric (ME) coupling due to magnetic V doping. The existence of magnetoelectric coupling without long-range magnetic order is of fundamental interest for advancing the understanding and development of ME coupling.
Modulating the Optical Properties of Cationic Surfactant Cetylpyridinium Chloride and Hydrazine Mediated Copper Nanoclusters Shashi Shekhar, Khokan Paria, Sameeksha Agrawal, Saptarshi Mukherjee Chemphyschem, 2025 This study investigates the modulations in the optical properties of cationic surfactant cetylpyridinium chloride (CPC) and hydrazine‐mediated copper nanoclusters (CuNCs). By employing a bottom‐up approach, we demonstrate the formation of blue‐emitting CuNCs facilitated by CPC and hydrazine, where hydrazine acts both as a reducing and stabilizing agent. The optical properties of the CuNCs were systematically tuned by varying the chain length of the diamine, resulting in emissions ranging from blue to yellow. Comprehensive characterization using spectroscopic and microscopic techniques confirmed the successful formation of CuNCs and elucidated the roles of CPC and hydrazine in their preparation. Control experiments highlighted the critical role of the pyridinium moiety and hydrophobic chain of CPC in enhancing the photoluminescence properties of the CuNCs. This work provides new insights into the design of stable, highly luminescent CuNCs for potential applications in optoelectronics and bioimaging.
Effect of β-CD on refolding dynamics of the unfolded and reduced states of human serum albumin Indian Journal of Chemistry Section A Inorganic Physical Theoretical and Analytical Chemistry, 2013
Binding interactions of β-carboline drugs with B-isoform of human serum albumin: Spectroscopic and thermodynamic investigations D Shil, R Yadav, S Rai, S Mukherjee Journal of Chemical Sciences 138 (2), 57 , 2026 2026
Critical processing parameters and advanced characterization of electrospun nanofiber scaffolds for drug delivery and biomedical applications S Mukherjee, S Ghatole, D Bhattacharyya, S Kaity Chemical Physics Impact, 101080 , 2026 2026
Fundamental assembly to performance cues of granular hydrogel based therapeutics for advanced biomedical applications S Das, S Mukherjee, S Roy, S Kaity European Polymer Journal, 114647 , 2026 2026
Progress in biopolymer-based polyelectrolyte complexes for biomedical applications D Bhattacharyya, S Mukherjee, S Kaity Reactive and Functional Polymers, 106731 , 2026 2026 Citations: 1
Association Interactions of Hydroxychloroquine Sulfate With DMPG Liposomes: CTAB‐Induced Lipid Solubilization and Subsequent Drug Release R Yadav, S Das, D Shil, S Mukherjee Chemistry–An Asian Journal 21 (2), e70589 , 2026 2026
Esterase-like “Superactivity” of Apo-Human Serum Transferrin: Specific Role of Hydrophobic Tail Chain Length and Charge of Headgroup of Surfactants R Yadav, S Das, S Ghosh, D Shil, A Pyne, S Mukherjee Biochemistry 65 (1), 77-89 , 2025 2025 Citations: 1
Effect of Water–DMSO Binary Solvent Mixture on the Behavior of an Intrinsically Disordered Protein, β-Casein S Rai, D Shil, BK Paul, S Mukherjee The Journal of Physical Chemistry B 129 (44), 11363-11373 , 2025 2025 Citations: 2
Impact of Intrinsic Hydrophobicity of Bile Salts on the Inhibition of Temperature‐Induced Aggregation of Bovine Serum Albumin R Yadav, A Nandy, D Biswas, S Mukherjee ChemPhysChem 26 (20), e202500460 , 2025 2025 Citations: 3
Intracellular Subdegree Temperature Sensing and Dynamics by Thermoresponsive Silver Nanoclusters as Molecular Probes S Rai, S Agrawal, S Mukherjee The Journal of Physical Chemistry Letters 16 (36), 9316-9324 , 2025 2025 Citations: 2
Modulating the spectroscopic signatures of gold nanoclusters: The role of hydrophobicity of bile salts N Mohite, K Paria, P Mahato, S Mukherjee Journal of Surfactants and Detergents 28 (5), 1115-1126 , 2025 2025 Citations: 1
Recent drug delivery systems targeting the gut-brain-microbiome axis for the management of chronic diseases D Ray, P Bose, S Mukherjee, S Roy, S Kaity International Journal of Pharmaceutics 680, 125776 , 2025 2025 Citations: 7
Modulating the optical properties of cationic surfactant cetylpyridinium chloride and hydrazine mediated copper nanoclusters S Shekhar, K Paria, S Agrawal, S Mukherjee ChemPhysChem 26 (6), e202401021 , 2025 2025 Citations: 1
Cyclodextrin Derivatives as Modulators for Enhanced Drug Delivery from Niosome Membrane: A Fluorescence Correlation Spectroscopy and Isothermal Titration Calorimetry Approach S Rai, M Mukherjee, BK Paul, S Mukherjee Langmuir 41 (3), 1601-1613 , 2025 2025 Citations: 4
Probing the nucleobase-specific binding interaction of hydroxychloroquine sulfate with RNA and subsequent sequestration by a water-soluble molecular basket R Yadav, S Das, M Mukherjee, S Mukherjee Physical Chemistry Chemical Physics 27 (14), 7365-7374 , 2025 2025 Citations: 7
Multi-source Flood Event Inventory A Mallick, S Ghosh, S Saha, J Mukherjee, S Mukherjee, A Chowdhury, ... AGU24 , 2024 2024
Micro‐Ring Morphology of Ag 7 NCs and Light‐Induced Reversible Interconversion of FCC Ag 14 NCs via Cu 2+ ions‐Mediated Particle‐Assisted Reversible … P Mahato, K Mandal, K Paria, D Chopra, S Mukherjee Angewandte Chemie 136 (40), e202409141 , 2024 2024 Citations: 4
Photoinduced formation and intercluster conversion of a thiol-templated copper nanocluster R Gupta, S Agrawal, S Rai, J Sarkar, S Kumari, D Shil, S Mukherjee ACS Applied Optical Materials 2 (9), 1880-1890 , 2024 2024 Citations: 11
Fabrication and optimization of extended-release beads of diclofenac sodium based on Ca plus plus cross-linked Taro ( Colocasia esculenta ) stolon … S Sarkar, S Manna, E Das, P Jana, S Mukherjee, R Sahu, TK Dua, P Paul, ... INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 271 , 2024 2024
Erratum to Editorial—Dynamics in complex chemical systems (2022) 4/100084 S Mukherjee Chemical Physics Impact 8, 100624 , 2024 2024
Assemble–Disassemble–Reassemble Dynamics in Copper Nanocluster-Based Superstructures S Agrawal, S Rai, P Mahato, A Ali, S Mukherjee The Journal of Physical Chemistry Letters 15 (18), 4880-4889 , 2024 2024 Citations: 11
MOST CITED SCHOLAR PUBLICATIONS
Luminescent copper nanoclusters as a specific cell-imaging probe and a selective metal ion sensor NK Das, S Ghosh, A Priya, S Datta, S Mukherjee The Journal of Physical Chemistry C 119 (43), 24657-24664 , 2015 2015 Citations: 189
Exploring the mechanism of fluorescence quenching in proteins induced by tetracycline U Anand, C Jash, RK Boddepalli, A Shrivastava, S Mukherjee The Journal of Physical Chemistry B 115 (19), 6312-6320 , 2011 2011 Citations: 177
Spectroscopic probing of the microenvironment in a protein− surfactant assembly U Anand, C Jash, S Mukherjee The Journal of Physical Chemistry B 114 (48), 15839-15845 , 2010 2010 Citations: 176
Binding interaction of a prospective chemotherapeutic antibacterial drug with β-lactoglobulin: results and challenges BK Paul, N Ghosh, S Mukherjee Langmuir 30 (20), 5921-5929 , 2014 2014 Citations: 121
Protein-protected metal nanoclusters as diagnostic and therapeutic platforms for biomedical applications I Zare, DM Chevrier, A Cifuentes-Rius, N Moradi, Y Xianyu, S Ghosh, ... Materials Today 66, 159-193 , 2023 2023 Citations: 119
Reversibility in protein folding: effect of β-cyclodextrin on bovine serum albumin unfolded by sodium dodecyl sulphate U Anand, S Mukherjee Physical Chemistry Chemical Physics 15 (23), 9375-9383 , 2013 2013 Citations: 119
Spectroscopic determination of Critical Micelle Concentration in aqueous and non-aqueous media using a non-invasive method U Anand, C Jash, S Mukherjee Journal of colloid and interface science 364 (2), 400-406 , 2011 2011 Citations: 108
Binding, unfolding and refolding dynamics of serum albumins U Anand, S Mukherjee Biochimica et Biophysica Acta (BBA)-General Subjects 1830 (12), 5394-5404 , 2013 2013 Citations: 107
Hydrophobicity is the governing factor in the interaction of human serum albumin with bile salts N Ghosh, R Mondal, S Mukherjee Langmuir 31 (3), 1095-1104 , 2015 2015 Citations: 105
Interplay of multiple interaction forces: binding of norfloxacin to human serum albumin BK Paul, N Ghosh, S Mukherjee The Journal of Physical Chemistry B 119 (41), 13093-13102 , 2015 2015 Citations: 104
Photostable copper nanoclusters: Compatible forster resonance energy-transfer assays and a nanothermometer S Ghosh, NK Das, U Anand, S Mukherjee The Journal of Physical Chemistry Letters 6 (7), 1293-1298 , 2015 2015 Citations: 93
Toggling between blue-and red-emitting fluorescent silver nanoclusters U Anand, S Ghosh, S Mukherjee The Journal of Physical Chemistry Letters 3 (23), 3605-3609 , 2012 2012 Citations: 89
Solvation dynamics of 4-aminophthalimide in dioxane–water mixture S Mukherjee, K Sahu, D Roy, SK Mondal, K Bhattacharyya Chemical physics letters 384 (1-3), 128-133 , 2004 2004 Citations: 85
Luminescent silver nanoclusters acting as a label-free photoswitch in metal ion sensing S Ghosh, U Anand, S Mukherjee Analytical chemistry 86 (6), 3188-3194 , 2014 2014 Citations: 83
Protein unfolding and subsequent refolding: a spectroscopic investigation U Anand, C Jash, S Mukherjee Physical Chemistry Chemical Physics 13 (45), 20418-20426 , 2011 2011 Citations: 81
Deciphering the role of pH in the binding of ciprofloxacin hydrochloride to bovine serum albumin U Anand, L Kurup, S Mukherjee Physical Chemistry Chemical Physics 14 (12), 4250-4258 , 2012 2012 Citations: 80
Fluorescent metal nano-clusters as next generation fluorescent probes for cell imaging and drug delivery K Bhattacharyya, S Mukherjee Bulletin of the Chemical Society of Japan 91 (3), 447-454 , 2018 2018 Citations: 75
Interaction of bile salts with β-cyclodextrins reveals nonclassical hydrophobic effect and enthalpy–entropy compensation BK Paul, N Ghosh, S Mukherjee The Journal of Physical Chemistry B 120 (16), 3963-3968 , 2016 2016 Citations: 67
Inverse temperature dependence in static quenching versus calorimetric exploration: binding interaction of chloramphenicol to β-lactoglobulin N Ghosh, R Mondal, S Mukherjee Langmuir 31 (29), 8074-8080 , 2015 2015 Citations: 63
Solvation dynamics in the water pool of an aerosol-OT microemulsion. Effect of sodium salicylate and sodium cholate P Dutta, P Sen, S Mukherjee, A Halder, K Bhattacharyya The Journal of Physical Chemistry B 107 (39), 10815-10822 , 2003 2003 Citations: 61
