Fluorescence Investigation on the Interaction of a Prevalent Competitive Fluorescent Probe with Entomic Odorant Binding Protein

Li, Hongliang; Zhang, Linya; Zhuang, Shulin; Ni, Cuixia; Shang, Hanwu

doi:10.1080/00387010.2013.763830

Cited by 5 publications

(2 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…NPN fluorescence of BSA samples was carried out on the Perkin-Elmer LS55 spectrofluorimeter using 60 μM aqueous solution of NPN fluorophore [ 33 ]. Fluorescence spectra were recorded with 1.5 μM of protein samples in the range of 370–600 nm.…”

Section: Materials and Methodologymentioning

confidence: 99%

Ribosylation induced structural changes in Bovine Serum Albumin: understanding high dietary sugar induced protein aggregation and amyloid formation

Das

Basak

Pramanik

et al. 2020

Heliyon

View full text Add to dashboard Cite

Non-enzymatic glycation of proteins is believed to be the root cause of high dietary sugar associated pathophysiological maladies. We investigated the structural changes in protein during progression of glycation using ribosylated Bovine Serum Albumin (BSA). Non enzymatic attachment of about 45 ribose molecules to BSA resulted in gradual reduction of hydrophobicity and aggregation as indicated by red-shifted tryptophan fluorescence, reduced ANS binding and lower anisotropy of FITC-conjugated protein. Parallely, there was a significant decrease of alpha helicity as revealed by Circular Dichroism (CD) and Fourier transformed-Infra Red (FT-IR) spectra. The glycated proteins assumed compact globular structures with enhanced Thioflavin-T binding resembling amyloids. The gross structural transition affected by ribosylation led to enhanced thermostability as indicated by melting temperature and Transmission Electron Microscopy. At a later stage of glycation, the glycated proteins developed non-specific aggregates with increase in size and loss of amyloidogenic behaviour. A parallel non-glycated control incubated under similar conditions indicated that amyloid formation and associated changes were specific for ribosylation and not driven by thermal denaturation due to incubation at 37 °C. Functionality of the glycated protein was significantly altered as probed by Isothermal Titration Calorimetry using polyphenols as substrates. The studies demonstrated that glycation driven globular amyloids form and persist as transient intermediates during formation of misfolded glycated adducts. To the best of our knowledge, the present study is the first systematic attempt to understand glycation associated changes in a protein and provides important insights towards designing therapeutics for arresting dietary sugar induced amyloid formation.

show abstract

Section: Materials and Methodologymentioning

confidence: 99%

Ribosylation induced structural changes in Bovine Serum Albumin: understanding high dietary sugar induced protein aggregation and amyloid formation

Das

Basak

Pramanik

et al. 2020

Heliyon

View full text Add to dashboard Cite

show abstract

“…They suggest that these interactions can occur through benzene rings even with Tyr109 and Tyr117 as hydrophilic residues. To date, only 12 studies that have performed molecular docking on the homology models of insect OBPs, and which include the relevant information about key residues for ligand binding, have been published (Honson et al , ; Jiang et al , ; Biessmann et al , ; Rusconi et al , ; Yu et al, ; Zhang et al , ; Li et al , ; Wang et al , ; Yu & Plettner, ; Lu et al , ; Jayanthi, P.D.K. et al , ; Zhuang et al , ) (Table ).…”

Section: Methodsmentioning

confidence: 99%

Ligand binding and homology modelling of insect odorant‐binding proteins

et al. 2014

View full text Add to dashboard Cite

Abstract. This review describes the main characteristics of odorant-binding proteins (OBPs) for homology modelling and presents a summary of structure prediction studies on insect OBPs, along with the steps involved and some limitations and improvements. The technique involves a computing approach to model protein structures and is based on a comparison between a target (unknown structure) and one or more templates (experimentally determined structures). As targets for structure prediction, OBPs are considered to play a functional role for recognition, desorption, scavenging, protection and transportation of hydrophobic molecules (odourants) across an aqueous environment (lymph) to olfactory receptor neurones (ORNs) located in sensilla, the main olfactory units of insect antennae. Lepidopteran pheromone-binding proteins, a subgroup of OBPs, are characterized by remarkable structural features, in which high sequence identities (approximately 30%) among these OBPs and a large number of available templates can facilitate the prediction of precise homology models. Approximately 30 studies have been performed on insect OBPs using homology modelling as a tool to predict their structures. Although some of the studies have assessed ligand-binding affinity using structural information and biochemical measurements, few have performed docking and molecular dynamic (MD) simulations as a virtual method to predict best ligands. Docking and MD simulations are discussed in the context of discovery of novel semiochemicals (super-ligands) using homology modelling to conceive further strategies in insect management.

show abstract