title: Structural elucidation of estrus urinary lipocalin protein (EULP) and evaluating binding affinity with pheromones using molecular docking and fluorescence study.
abstract: Transportation of pheromones bound with carrier proteins belonging to lipocalin superfamily is known to prolong chemo-signal communication between individuals belonging to the same species. Members of lipocalin family (MLF) proteins have three structurally conserved motifs for delivery of hydrophobic molecules to the specific recognizer. However, computational analyses are critically required to validate and emphasize the sequence and structural annotation of MLF. This study focused to elucidate the evolution, structural documentation, stability and binding efficiency of estrus urinary lipocalin protein (EULP) with endogenous pheromones adopting in-silico and fluorescence study. The results revealed that: (i) EULP perhaps originated from fatty acid binding protein (FABP) revealed in evolutionary analysis; (ii) Dynamic simulation study shows that EULP is highly stable at below 0.45 Å of root mean square deviation (RMSD); (iii) Docking evaluation shows that EULP has higher binding energy with farnesol and 2-iso-butyl-3-methoxypyrazine (IBMP) than 2-naphthol; and (iv) Competitive binding and quenching assay revealed that purified EULP has good binding interaction with farnesol. Both, In-silico and experimental studies showed that EULP is an efficient binding partner to pheromones. The present study provides impetus to create a point mutation for increasing longevity of EULP to develop pheromone trap for rodent pest management.
authors: Centre for Pheromone Technology, Department of Animal Science, School of Life Sciences, Bharathidasan University, Tiruchirappalli-620 024, India.|Research Institute in Semiochemistry and Applied Ethology (IRSEA), Quartier Salignan, 84400, APT, France.
authors: Durairaj
authors: D
authors: Rajesh
authors: Centre for Pheromone Technology, Department of Animal Science, School of Life Sciences, Bharathidasan University, Tiruchirappalli-620 024, India.|Centre for Animal Research, Training and Services (CAReTS), Central Inter-Disciplinary Research Facility (CIDRF), Mahatma Gandhi Medical College and Research Institute (MGMC-RI) Campus, Puducherry-607403, India.
authors: Subramanian
authors: S
authors: Muthukumar
authors: Centre for Pheromone Technology, Department of Animal Science, School of Life Sciences, Bharathidasan University, Tiruchirappalli-620 024, India.|National Centre for Alternatives to Animal Experiments, Bharathidasan University, Tiruchirappalli-620 024, India.
authors: Ganesan
authors: G
authors: Saibaba
authors: National Centre for Alternatives to Animal Experiments, Bharathidasan University, Tiruchirappalli-620 024, India.|Department of Environmental Biotechnology, Bharathidasan University, Tiruchirappalli-620 024, India.
authors: Durairaj
authors: D
authors: Siva
authors: National Centre for Alternatives to Animal Experiments, Bharathidasan University, Tiruchirappalli-620 024, India.|Department of Food Science and Nutrition, College of Food Science and Agriculture, King Saud University, Riyadh, Kingdom of Saudi Arabia.
authors: Mohammad Abdulkader
authors: MA
authors: Akbarsha
authors: Lee Kong Chian School of Medicine, Nanyang Technological University-636921, Singapore.
authors: Balázs
authors: B
authors: Gulyás
authors: Lee Kong Chian School of Medicine, Nanyang Technological University-636921, Singapore.
authors: Parasuraman
authors: P
authors: Padmanabhan
authors: Centre for Pheromone Technology, Department of Animal Science, School of Life Sciences, Bharathidasan University, Tiruchirappalli-620 024, India.|National Centre for Alternatives to Animal Experiments, Bharathidasan University, Tiruchirappalli-620 024, India.
authors: Govindaraju
authors: G
authors: Archunan
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001667:Binding, Competitive; D004971:Estrus / Q000652:urine*; D050556:Fatty Acid-Binding Proteins / Q000378:metabolism; D005260:Female; D008024:Ligands; D054834:Lipocalins / Q000737:chemistry / Q000235:genetics / Q000652:urine*; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D010675:Pheromones / Q000378:metabolism; D010802:Phylogeny; D011485:Protein Binding; D060066:Protein Interaction Maps; D051381:Rats; D013050:Spectrometry, Fluorescence
chemical_list: D050556:Fatty Acid-Binding Proteins; D008024:Ligands; D054834:Lipocalins; D010675:Pheromones