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Enhanced DR5 binding capacity of nanovectorized TRAIL compared to its cytotoxic version by affinity chromatography and molecular docking studies.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Zakaria, Albatoul Picaud, Fabien Guillaume, Yves Claude Gharbi, Tijani Micheau, Olivier Herlem, Guillaume
Description	Country affiliation: France Author Affiliation: Zakaria A ( NanoMedicine, Imagery and Therapeutics Lab EA 4662, University of Franche-Comte, CHU Jean Minjoz, 25030, Besançon cedex, France.); Picaud F ( NanoMedicine, Imagery and Therapeutics Lab EA 4662, University of Franche-Comte, CHU Jean Minjoz, 25030, Besançon cedex, France.); Guillaume YC ( NanoMedicine, Imagery and Therapeutics Lab EA 4662, University of Franche-Comte, CHU Jean Minjoz, 25030, Besançon cedex, France.); Gharbi T ( NanoMedicine, Imagery and Therapeutics Lab EA 4662, University of Franche-Comte, CHU Jean Minjoz, 25030, Besançon cedex, France.); Micheau O ( INSERM, UMR866, Faculty of Medicine and Pharmacy, Burgundy University, Dijon, F-21079, France.)
Abstract	Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induces apoptosis of cancer cells when bound to its cognate receptors, TRAIL-R1 and TRAIL-R2 (DR4 and DR5), without being toxic to healthy cells. Nanovectorized TRAIL (abbreviated as NPT) is 10 to 20 times more efficient than one of the most potent soluble TRAIL used in preclinical studies (His-TRAIL). To determine whether differences in affinity may account for NPT superiority, a thermodynamic study was undertaken to evaluate NPT versus TRAIL binding affinity to DR5. Docking calculations showed that TRAIL in homotrimer configuration was more stable than in heterotrimer, because of the presence of one Zn ion in its structure. Indeed, TRAIL trimers can have head-to-tail orientations when Zn is missing. Altogether these data suggest that TRAIL homotrimer structures are predominant in solution and then are grafted on NPT. When docked to DR5, NPT carrying TRAIL homotrimer leads to a more stable complex than TRAIL monomer-based NPT. To comfort these observations, the extracellular domain of DR5 was immobilized on a chromatographic support using an 'in situ' immobilization technique. The determination of the thermodynamic data (enthalpy ∆H° and entropy ∆S°) of TRAIL and NPT binding to DR5 showed that the binding mechanism was pH dependent. The affinity of NPT to DR5 increased with pH, and the ionized energy was more important for NPT than for soluble TRAIL. Moreover, because of negative values of ∆H° and ∆S° quantities, we demonstrated that van der Waals and hydrogen bonds governed the strong NPT-DR5 association for pH > 7.4 (as for TRAIL alone). Copyright © 2016 John Wiley & Sons, Ltd.
File Format	HTM / HTML
ISSN	09523499
Issue Number	9
Journal	Journal of Molecular Recognition
Volume Number	29
e-ISSN	10991352
Language	English
Publisher	Wiley
Publisher Date	2016-09-01
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology

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