Dr. Satish Mutyala is working as an assistant professor at the School of Sciences at Woxsen University Hyderabad. In 2016, He received his M.Tech (Medical Biotechnology) from the Indian Institute of Technology. In 2016, enrolled as a Ph.D. student at the Indian Institute of Technology Hyderabad (IIT Hyderabad), Department of Biotechnology, and worked under the supervision of Dr. Rajakumara Eerappa; he has awarded a doctoral degree with a thesis entitled “Phosphodiesterase structure-based design of pentoxifylline analogues, and computational and biochemical evaluation of pentoxifylline analogues and xanthine derivatives against phosphodiesterases functioning in
Skilled in Biotechnology research, Biophysical binding assays, Drug Design and Development, molecular modelling, and molecular dynamic simulations.
EDUCATION
PhD in Biotechnology
RESEARCH, TEACHING, or OTHER INTERESTS
Biotechnology, Structural Biology, General Biochemistry, Genetics and Molecular Biology, Drug Discovery
9
Scopus Publications
Scopus Publications
Biofilm (Eco-Corona) Formation from Microplastics in Freshwater Mutyala Satish, Sourav Maity Handbook of Microplastic Pollution in the Environment Microplastic Pollution in Aquatic Environments, 2025 Eco-corona formation, commonly referred to as biofilm formation from microplastics, has become a major worry in freshwater environments. Freshwater habitats are rife with microplastics, which pose major threats to the environment and public health. Microplastics, which are tiny plastic particles less than 5 mm, offer a good substrate for the development of biofilms because of their substantial surface area and hydrophobic nature. Microplastics undergo physical, chemical, and biological changes when they enter freshwater systems, which causes a biofilm layer to grow. Extracellular polymeric substances (EPS), other organic materials, and microbial communities are all assembled into a complex matrix during the biofilm development process by the adsorption of organic and inorganic components onto the microplastic surface. Depending on the environmental factors, the biofilm growth on microplastics can happen quickly, in only a few hours to a few days. Their destiny and transportation in freshwater ecosystems are impacted by biofilm formation on microplastics. Microplastics’ physical and chemical characteristics, including their buoyancy, aggregation patterns, and capacity for sorption of other contaminants, are altered by the eco-corona. Additionally, biofilms have the ability to influence the entire ecosystem by facilitating the ingestion and transport of microplastics within aquatic food webs. The production of biofilms from microplastics has severe ecological repercussions. Biofilms encourage the development and survival of microorganisms, which could result in the spread of dangerous germs and the modification of microbial communities. Antibiotic resistance in aquatic environments may be made worse by the increased colonization of microplastics by biofilms, which may also make it easier for antibiotic resistance genes to spread. The risk of waterborne diseases may also be increased by the formation of biofilms on microplastics, which may encourage the growth and persistence of pathogenic bacteria. Interdisciplinary research efforts and comprehensive management techniques are necessary to create successful strategies to limit the effects of microplastics on freshwater ecosystems, and this requires an understanding of the dynamics and ecological effects of the eco-corona.
Interaction of Secondary Micro(nano)plastics with Emerging Pollutants Mutyala Satish, Dipak Kumar Sahoo, Sourav Maity Handbook of Microplastic Pollution in the Environment Monitoring and Treatment of Microplastics and Policy Perspectives, 2025 Considering the potential effects on the environment and public health, the interaction between secondary micro(nano)plastics and emerging contaminants has attracted more and more attention in recent years. The deterioration and fragmentation of more oversized plastic objects produce secondary micro(nano)plastics, which have drawn much attention as the carriers and vectors of emerging contaminants in different ecosystems. The surface area, hydrophobicity, and electrostatic charge of secondary micro(nano)plastics, among other physicochemical characteristics, are critical in mediating the sorption, desorption, and transport of emerging contaminants. On the plastic surface, functional groups and sorption sites further increase the surface’s attraction to contaminants. Pharmaceuticals, cosmetics, insecticides, and industrial chemicals are a few sources of emerging contaminants with detrimental qualities frequently found in aquatic habitats. Secondary micro(nano)plastics can act as sorbents and transporters when these contaminants come into contact with them, enhancing their movement and possible bioaccumulation in various environmental compartments. Complex fate and transport mechanisms may result from interacting secondary micro(nano)plastics with emerging contaminants in various environmental matrices, including water, soil, sediments, and biota. These interactions could cause pollutants to be concentrated and adsorb to the plastic surface, potentially altering their bioavailability and toxicity. In addition, the aggregation and agglomeration of secondary micro(nano)plastics with adsorbed contaminants can promote their transit and deposition in different environmental compartments. Impacts on the environment and public health are also a result of the interplay between secondary micro(nano)plastics and emerging contaminants. Bioaccumulation and biomagnification of plastic-associated contaminants by creatures at various trophic levels have the potential to have negative effects on ecosystem dynamics. Additionally, ingesting plastic particles by organisms can cause physical harm, expose them to toxins inside, and cause pollutants to move up the food chain, endangering human health. Analytical methods, modeling, and risk assessment methodologies must address the complicated interactions between secondary micro(nano)plastics and emerging contaminants. Efforts should be made to reduce the sources of developing pollutants and the exposure of micro(nano)plastics to the environment. To solve this intricate environmental problem, proactive strategies are required, such as better waste management procedures and the development of eco-friendly substitutes.
Nanoparticle-Assisted Abiotic Remediation of Contaminated Soil Hannah Jebarani D. Angelene, Nitish Venkateswarlu Mogili, R. A. Zerubabel Michael, Mutyala Satish, Rajeswara Reddy Erva Plant Based Nanoparticle Synthesis for Sustainable Agriculture, 2025 Soil contamination is an alarming environmental issue arising from anthropogenic activity and agricultural practices. It poses substantial risks to human health and ecosystems. Conventional remediation methods have limitations in terms of the costs of treatments, contaminant removal efficiency, and environmental sustainability. Nanomaterial-assisted abiotic remediation has emerged as a sustainable approach, which involves the utilization of nanomaterials to address the complexities of contaminated soil remediation. This chapter provides an overview of different types of pollutants encountered in contaminated soil. It also examines the potential of different mechanisms (nano-immobilization, nano-adsorption, nanocatalysis, etc.) that apply nanomaterials for the remediation of contaminated soil. In addition, the ability of nanomaterials to detect contaminants (nanosensing) is detailed. Further, the fate of nanomaterials upon application in soil is highlighted and the potential of nanotechnology in addressing the environmental challenges involved in the remediation of contaminated soil is discussed.
Computational, biochemical and ex vivo evaluation of xanthine derivatives against phosphodiesterases to enhance the sperm motility Mutyala Satish, Kumari Sandhya, Kulhar Nitin, Ninjoor Yashas Kiran, Babu Aleena, Adiga Satish Kumar, Kalthur G, Eerappa Rajakumara Journal of Biomolecular Structure and Dynamics, 2023 Enhancing sperm motility in vitro has immensely benefited assisted conception methods. Phosphodiesterases (PDE) break the second messenger cAMP, and therefore, inhibition of their catalytic activity enhances the sperm motility through maintaining cAMP homeostasis in sperm. In view of identifying the molecules that could inhibit PDE functioning in spermatozoa, we aimed to evaluate the phosphodiesterase inhibitors (PDEI) - xanthine derivatives - acefylline, dyphylline and proxyphylline to repurpose them for assisted reproductive technology. These are available in the market as pharmaceutical agents to treat mainly respiratory system diseases. Based on the structure guided in silico studies, we predicted that these molecules bind to the cAMP binding catalytic pocket of PDE enzymes, and further molecular dynamics simulation analysis indicated that these molecules form the stable complexes. Isothermal titration calorimetry studies revealed that acefylline has better affinity towards PDE4A, PDE4D and PDE10A, when compared to dyphylline and proxyphylline. In addition, ex vivo studies corroborated in vitro binding studies that acefylline has much superior sperm motility enhancement property on human ejaculated spermatozoa and mouse testicular spermatozoa compared to dyphylline and proxyphylline. Communicated by Ramaswamy H. Sarma
Structure-based redesigning of pentoxifylline analogs against selective phosphodiesterases to modulate sperm functional competence for assisted reproductive technologies Mutyala Satish, Sandhya Kumari, Waghela Deeksha, Suman Abhishek, Kulhar Nitin, Satish Kumar Adiga, Padmaraj Hegde, Jagadeesh Prasad Dasappa, Guruprasad Kalthur, Eerappa Rajakumara Scientific Reports, 2021 Phosphodiesterase (PDE) inhibitors, such as pentoxifylline (PTX), are used as pharmacological agents to enhance sperm motility in assisted reproductive technology (ART), mainly to aid the selection of viable sperm in asthenozoospermic ejaculates and testicular spermatozoa, prior to intracytoplasmic sperm injection (ICSI). However, PTX is reported to induce premature acrosome reaction (AR) and, exert toxic effects on oocyte function and early embryo development. Additionally, in vitro binding studies as well as computational binding free energy (ΔGbind) suggest that PTX exhibits weak binding to sperm PDEs, indicating room for improvement. Aiming to reduce the adverse effects and to enhance the sperm motility, we designed and studied PTX analogues. Using structure-guided in silico approach and by considering the physico-chemical properties of the binding pocket of the PDEs, designed analogues of PTX. In silico assessments indicated that PTX analogues bind more tightly to PDEs and form stable complexes. Particularly, ex vivo evaluation of sperm treated with one of the PTX analogues (PTXm-1), showed comparable beneficial effect at much lower concentration—slower AR, higher DNA integrity and extended longevity of spermatozoa and superior embryo quality. PTXm-1 is proposed to be a better pharmacological agent for ART than PTX for sperm function enhancement.
Dynamic Basis for Auranofin Drug Recognition by Thiol-Reductases of Human Pathogens and Intermediate Coordinated Adduct Formation with Catalytic Cysteine Residues Suman Abhishek, Sreeragh Sivadas, Mutyala Satish, Waghela Deeksha, Eerappa Rajakumara ACS Omega, 2019 In all the living systems, reactive oxygen species (ROS) metabolism provides resistance against internal and external oxidative stresses. Auranofin (AF), an FDA-approved gold [Au(I)]-conjugated drug, is known to selectively target thiol-reductases, key enzymes involved in ROS metabolism. AF has been successfully tested for its inhibitory activity through biochemical studies, both in vitro and in vivo, against a diverse range of pathogens including protozoa, nematodes, bacteria, and so forth. Cocrystal structures of thiol-reductases complexed with AF revealed that Au(I) was coordinately linked to catalytic cysteines, but the mechanism of transfer of Au(I) from AF to catalytic cysteines still remains unknown. In this study, we have employed computational approaches to understand the interaction of AF with thiol-reductases of selected human pathogens. A similar network of interactions of AF was observed in all the studied enzymes. Also, we have shown that tailor-made analogues of AF can be designed against selective thiol-reductases for targeted inhibition. Molecular dynamics studies show that the AF-intermediates, tetraacetylthioglucose (TAG)-gold, and triethylphosphine (TP)-gold, coordinately linked to one of catalytic cysteines, remain stable in the binding pocket of thiol-reductases for Leishmania infantum and Plasmodium falciparum (PfTrxR). This suggests that the TP and TAG moieties of AF may be sequentially eliminated during the transfer of Au(I) to catalytic cysteines of the receptor.
Computational characterization of substrate and product specificities, and functionality of S-adenosylmethionine binding pocket in histone lysine methyltransferases from Arabidopsis, rice and maize Mutyala Satish, M. Angel Nivya, Suman Abhishek, Naveen Kumar Nakarakanti, Dixit Shivani, Madishetti Vinuthna Vani, Eerappa Rajakumara Proteins Structure Function and Bioinformatics, 2018 Histone lysine methylation by histone lysine methyltransferases (HKMTs) has been implicated in regulation of gene expression. While significant progress has been made to understand the roles and mechanisms of animal HKMT functions, only a few plant HKMTs are functionally characterized. To unravel histone substrate specificity, degree of methylation and catalytic activity, we analyzed Arabidopsis Trithorax‐like protein (ATX), Su(var)3‐9 homologs protein (SUVH), Su(var)3‐9 related protein (SUVR), ATXR5, ATXR6, and E(Z) HKMTs of Arabidopsis, maize and rice through sequence and structure comparison. We show that ATXs may exhibit methyltransferase specificity toward histone 3 lysine 4 (H3K4) and might catalyse the trimethylation. Our analyses also indicate that most SUVH proteins of Arabidopsis may bind histone H3 lysine 9 (H3K9). We also predict that SUVH7, SUVH8, SUVR1, SUVR3, ZmSET20 and ZmSET22 catalyse monomethylation or dimethylation of H3K9. Except for SDG728, which may trimethylate H3K9, all SUVH paralogs in rice may catalyse monomethylation or dimethylation. ZmSET11, ZmSET31, SDG713, SDG715, and SDG726 proteins are predicted to be catalytically inactive because of an incomplete S‐adenosylmethionine (SAM) binding pocket and a post‐SET domain. E(Z) homologs can trimethylate H3K27 substrate, which is similar to the Enhancer of Zeste homolog 2 of humans. Our comparative sequence analyses reveal that ATXR5 and ATXR6 lack motifs/domains required for protein‐protein interaction and polycomb repressive complex 2 complex formation. We propose that subtle variations of key residues at substrate or SAM binding pocket, around the catalytic pocket, or presence of pre‐SET and post‐SET domains in HKMTs of the aforementioned plant species lead to variations in class‐specific HKMT functions and further determine their substrate specificity, the degree of methylation and catalytic activity.
Mechanistic insights into the recognition of 5-methylcytosine oxidation derivatives by the SUVH5 SRA domain Eerappa Rajakumara, Naveen Kumar Nakarakanti, M. Angel Nivya, Mutyala Satish Scientific Reports, 2016 5-Methylcytosine (5 mC) is associated with epigenetic gene silencing in mammals and plants. 5 mC is consecutively oxidized to 5-hydroxymethylcytosine (5 hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC) by ten-eleven translocation enzymes. We performed binding and structural studies to investigate the molecular basis of the recognition of the 5 mC oxidation derivatives in the context of a CG sequence by the SET- and RING-associated domain (SRA) of the SUVH5 protein (SUVH5 SRA). Using calorimetric measurements, we demonstrate that the SRA domain binds to the hydroxymethylated CG (5hmCG) DNA duplex in a similar manner to methylated CG (5mCG). Interestingly, the SUVH5 SRA domain exhibits weaker affinity towards carboxylated CG (5caCG) and formylated CG (5fCG). We report the 2.6 Å resolution crystal structure of the SUVH5 SRA domain in a complex with fully hydroxymethyl-CG and demonstrate a dual flip-out mechanism, whereby the symmetrical 5hmCs are simultaneously extruded from the partner strands of the DNA duplex and are positioned within the binding pockets of individual SRA domains. The hydroxyl group of 5hmC establishes both intra- and intermolecular interactions in the binding pocket. Collectively, we show that SUVH5 SRA recognizes 5hmC in a similar manner to 5 mC, but exhibits weaker affinity towards 5 hmC oxidation derivatives.
