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

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 hydrophobi...

Full description

Saved in:
Bibliographic Details
Main Authors: Rajesh, Durairaj, Muthukumar, Subramanian, Saibaba, Ganesan, Siva, Durairaj, Akbarsha, Mohammad Abdulkader, Gulyás, Balázs, Padmanabhan, Parasuraman, Archunan, Govindaraju
Other Authors: Lee Kong Chian School of Medicine (LKCMedicine)
Format: Article
Language:English
Published: 2016
Subjects:
Online Access:https://hdl.handle.net/10356/84341
http://hdl.handle.net/10220/41787
Tags: Add Tag
No Tags, Be the first to tag this record!
Institution: Nanyang Technological University
Language: English
id sg-ntu-dr.10356-84341
record_format dspace
spelling sg-ntu-dr.10356-843412022-02-16T16:26:23Z Structural elucidation of estrus urinary lipocalin protein (EULP) and evaluating binding affinity with pheromones using molecular docking and fluorescence study Rajesh, Durairaj Muthukumar, Subramanian Saibaba, Ganesan Siva, Durairaj Akbarsha, Mohammad Abdulkader Gulyás, Balázs Padmanabhan, Parasuraman Archunan, Govindaraju Lee Kong Chian School of Medicine (LKCMedicine) Lee Kong Chian School of Medicine Proteome informatics Protein–protein interaction networks 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. Published version 2016-12-09T08:38:52Z 2019-12-06T15:43:08Z 2016-12-09T08:38:52Z 2019-12-06T15:43:08Z 2016 Journal Article Rajesh, D., Muthukumar, S., Saibaba, G., Siva, D., Akbarsha, M. A., Gulyás, B., et al. (2016). Structural elucidation of estrus urinary lipocalin protein (EULP) and evaluating binding affinity with pheromones using molecular docking and fluorescence study. Scientific Reports, 6, 35900-. 2045-2322 https://hdl.handle.net/10356/84341 http://hdl.handle.net/10220/41787 10.1038/srep35900 27782155 en Scientific Reports ©The Authors 2016. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ 14 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Proteome informatics
Protein–protein interaction networks
spellingShingle Proteome informatics
Protein–protein interaction networks
Rajesh, Durairaj
Muthukumar, Subramanian
Saibaba, Ganesan
Siva, Durairaj
Akbarsha, Mohammad Abdulkader
Gulyás, Balázs
Padmanabhan, Parasuraman
Archunan, Govindaraju
Structural elucidation of estrus urinary lipocalin protein (EULP) and evaluating binding affinity with pheromones using molecular docking and fluorescence study
description 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.
author2 Lee Kong Chian School of Medicine (LKCMedicine)
author_facet Lee Kong Chian School of Medicine (LKCMedicine)
Rajesh, Durairaj
Muthukumar, Subramanian
Saibaba, Ganesan
Siva, Durairaj
Akbarsha, Mohammad Abdulkader
Gulyás, Balázs
Padmanabhan, Parasuraman
Archunan, Govindaraju
format Article
author Rajesh, Durairaj
Muthukumar, Subramanian
Saibaba, Ganesan
Siva, Durairaj
Akbarsha, Mohammad Abdulkader
Gulyás, Balázs
Padmanabhan, Parasuraman
Archunan, Govindaraju
author_sort Rajesh, Durairaj
title Structural elucidation of estrus urinary lipocalin protein (EULP) and evaluating binding affinity with pheromones using molecular docking and fluorescence study
title_short Structural elucidation of estrus urinary lipocalin protein (EULP) and evaluating binding affinity with pheromones using molecular docking and fluorescence study
title_full Structural elucidation of estrus urinary lipocalin protein (EULP) and evaluating binding affinity with pheromones using molecular docking and fluorescence study
title_fullStr Structural elucidation of estrus urinary lipocalin protein (EULP) and evaluating binding affinity with pheromones using molecular docking and fluorescence study
title_full_unstemmed Structural elucidation of estrus urinary lipocalin protein (EULP) and evaluating binding affinity with pheromones using molecular docking and fluorescence study
title_sort structural elucidation of estrus urinary lipocalin protein (eulp) and evaluating binding affinity with pheromones using molecular docking and fluorescence study
publishDate 2016
url https://hdl.handle.net/10356/84341
http://hdl.handle.net/10220/41787
_version_ 1725985772171952128