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The role of surface charge in the desolvation process of gelatin: implications in nanoparticle synthesis and modulation of drug release

Authors Ahsan SM, Rao CM

Received 18 October 2016

Accepted for publication 3 December 2016

Published 24 January 2017 Volume 2017:12 Pages 795—808

DOI https://doi.org/10.2147/IJN.S124938

Checked for plagiarism Yes

Review by Single anonymous peer review

Peer reviewer comments 4

Editor who approved publication: Dr Thomas Webster


Saad M Ahsan, Chintalagiri Mohan Rao

Centre for Cellular and Molecular Biology, Council of Scientific and Industrial Research, Hyderabad, Telangana, India

Abstract: The process of moving hydrophobic amino acids into the core of a protein by desolvation is important in protein folding. However, a rapid and forced desolvation can lead to precipitation of proteins. Desolvation of proteins under controlled conditions generates nanoparticles – homogeneous aggregates with a narrow size distribution. The protein nanoparticles, under physiological conditions, undergo surface erosion due to the action of proteases, releasing the entrapped drug/gene. The packing density of protein nanoparticles significantly influences the release kinetics. We have investigated the desolvation process of gelatin, exploring the role of pH and desolvating agent in nanoparticle synthesis. Our results show that the desolvation process, initiated by the addition of acetone, follows distinct pathways for gelatin incubated at different pH values and results in the generation of nanoparticles with varying matrix densities. The nanoparticles synthesized with varying matrix densities show variations in drug loading and protease-dependent extra- and intracellular drug release. These results will be useful in fine-tuning the synthesis of nanoparticles with desirable drug release profiles.

Keywords: protein desolvation, nanoparticle assembly, gelatin nanoparticle synthesis, protease susceptibility, intracellular drug release

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