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Int. J. Mol. Sci. 2015, 16(8), 17289-17302;

Combined Spectroscopic and Calorimetric Studies to Reveal Absorption Mechanisms and Conformational Changes of Protein on Nanoporous Biomaterials

Department of Biology, Science and Research Branch, Islamic Azad University, Tehran P. O. Box: 1477893855, Iran
Department of Nanotechnology and Advanced materials, Materials and Energy Research Center, Tehran P. O. Box: 31787316, Iran
Department of Nanotechnology, Faculty of Advance Science and Technology, Islamic Azad University of Pharmaceutical Sciences (IAUPS), Tehran P. O. Box: 193956466, Iran
Author to whom correspondence should be addressed.
Academic Editor: Bernhard Schuster
Received: 20 March 2015 / Revised: 21 May 2015 / Accepted: 23 June 2015 / Published: 29 July 2015
(This article belongs to the Section Biochemistry, Molecular and Cellular Biology)
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In this study the effect of surface modification of mesoporous silica nanoparticles (MSNs) on its adsorption capacities and protein stability after immobilization of beta-lactoglobulin B (BLG-B) was investigated. For this purpose, non-functionalized (KIT-6) and aminopropyl-functionalized cubic Ia3d mesoporous silica ([n-PrNH2-KIT-6]) nanoparticles were used as nanoporous supports. Aminopropyl-functionalized mesoporous nanoparticles exhibited more potential candidates for BLG-B adsorption and minimum BLG leaching than non-functionalized nanoparticles. It was observed that the amount of adsorbed BLG is dependent on the initial BLG concentration for both KIT-6 and [n-PrNH2-KIT-6] mesoporous nanoparticles. Also larger amounts of BLG-B on KIT-6 was immobilized upon raising the temperature of the medium from 4 to 55 °C while such increase was undetectable in the case of immobilization of BLG-B on the [n-PrNH2-KIT-6]. At temperatures above 55 °C the amounts of adsorbed BLG on both studied nanomaterials decreased significantly. By Differential scanning calorimetry or DSC analysis the heterogeneity of the protein solution and increase in Tm may indicate that immobilization of BLG-B onto the modified KIT-6 results in higher thermal stability compared to unmodified one. The obtained results provide several crucial factors in determining the mechanism(s) of protein adsorption and stability on the nanostructured solid supports and the development of engineered nano-biomaterials for controlled drug-delivery systems and biomimetic interfaces for the immobilization of living cells. View Full-Text
Keywords: protein; nanoporous; immobilization; BLG-B; calorimetry protein; nanoporous; immobilization; BLG-B; calorimetry

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Ahmadi, S.; Farokhi, M.; Padidar, P.; Falahati, M. Combined Spectroscopic and Calorimetric Studies to Reveal Absorption Mechanisms and Conformational Changes of Protein on Nanoporous Biomaterials. Int. J. Mol. Sci. 2015, 16, 17289-17302.

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