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Updated: Dec 25, 2025

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
A Review of Properties, Delivery Systems and Analytical Methods for the Characterization of Monomeric Glycoprotein
Mariza Aires Fernandes1, Gilmar Hanck-Silva1, Franciele Garcia Baveloni1
1School of Pharmaceutical Sciences, São Paulo State University (UNESP), Araraquara, São Paulo, Brazil.
Abstract:
Transferrin is a protein involved in iron uptake by cells and has been identified as a potential target for directing drug-loaded nanoparticles for cancer treatment and diagnosis. Most methods for conjugation of transferrin and nanoparticles involve the formation of a thioeter bond between thiolated transferrin and maleimide-containing nanoparticle. For nanoparticle development, it is important to perform a thorough physicochemical characterization, including quantification of the amount of transferrin functionalizing the delivery system. Thus, following the transferrin and nanoparticle chemical conjugation, an analytical method is need for transferrin quantification. Altogether, we revised both physicochemical and pharmacokinetics transferrin characteristics, the aspects of iron transport after interaction with transferrin, the development of transferrin targeted-nanoparticles, highlighting both their composition, synthesis methods and in vitro/in vivo evaluation. Furthermore, we addressed the analytical methods employed in protein quantification, including spectrophotometric/colorimetric, immunoassays, electrophoretic and chromatographic techniques used to identify and/or quantify of transferrin in biological matrices and drug delivery systems.
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