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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Self-assembled carbohydrate-based vesicles for lectin targeting

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Author(s):
dos Santos, Marinalva Cardoso ; Serafini Micheletto, Yasmine Miguel ; da Silveira, Nadya Pesce ; Pinto, Luciano da Silva ; Giacomelli, Fernando Carlos ; de Lima, Vania Rodrigues ; Allievi Frizon, Tiago Elias ; Dal-Bo, Alexandre Goncalves
Total Authors: 8
Document type: Journal article
Source: COLLOIDS AND SURFACES B-BIOINTERFACES; v. 148, p. 12-18, DEC 1 2016.
Web of Science Citations: 4
Abstract

This study examined the physicochemical interactions between vesicles formed by phosphatidylcholine (PC) and glycosylated polymeric amphiphile N-acetyl-beta-D-glucosaminsrl-PEG(900)-docosanate (C(22)PEG(900)GIcNAc) conjugated with Bauhinia variegata lectin (BVL). Lectins are proteins or glycoproteins capable of binding glycosylated membrane components. Accordingly, the surface functionalization by such entities is considered a potential strategy for targeted drug delivery. We observed increased hydrodynamic radii (R-H) of PC+C(22)PEG(900)GlcNAc vesicles in the presence of lectins, suggesting that this aggregation was due to the interaction between lectins and the vesicular glycosylated surfaces. Furthermore, changes in the zeta potential of the vesicles with increasing lectin concentrations implied that the vesicular glycosylated surfaces were recognized by the investigated lectin. The presence of carbohydrate residues on vesicle surfaces and the ability of the vesicles to establish specific interactions with BVL were further explored using atomic force microscopy (AFM) and small-angle X-ray scattering (SAXS) analysis. The results indicated that the thickness of the hydrophilic layer was to some extent influenced by the presence of lectins. The presence of lectins required a higher degree of polydispersity as indicated by the width parameter of the log-normal distribution of size, which also suggested more irregular structures. Reflectance Fourier transform infrared (HATR-FTIR), differential scanning calorimetry (DSC), nuclear magnetic resonance (NMR) and ultraviolet-visible (UV-vis.) analyses revealed that the studied lectin preferentially interacted with the choline and carbonyl groups of the lipid, thereby changing the choline orientation and intermolecular interactions. The protein also discretely reduced the intermolecular communication of the hydrophobic acyl chains, resulting in a disordered state. (C) 2016 Elsevier B.V. All rights reserved. (AU)

FAPESP's process: 14/22983-9 - Development of nanostructured supramolecular polymer systems based on cationic block copolymer/DNA complexation with potential application in gene delivery
Grantee:Fernando Carlos Giacomelli
Support type: Regular Research Grants