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Sci Rep. 2016 Oct 26;6:35900. doi: 10.1038/srep35900.

Structural elucidation of estrus urinary lipocalin protein (EULP) and evaluating binding affinity with pheromones using molecular docking and fluorescence study.

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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.
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.
National Centre for Alternatives to Animal Experiments, Bharathidasan University, Tiruchirappalli-620 024, India.
Department of Environmental Biotechnology, 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.
Lee Kong Chian School of Medicine, Nanyang Technological University-636921, Singapore.


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.

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