Interaction Of Calcium Phosphate Nanoparticles With Human Chorionic Gonadotropin Modifies Secondary And Tertiary Protein Structure

Calcium phosphate nanoparticles (CaPNP) have good biocompatibility and bioactivity inside human body. In this study, the interaction between CaPNP and human chorionic gonadotropin (hCG) was analyzed to determine the changes in the protein structure in the presence of CaPNP and the quantity of protei...

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Main Authors: Al-Hakeim Hussein K, Al-Zabeba Rahman S., Grulke Eric, Jaffar Al-Mulla Emad A.
Format: Article
Language:English
Published: Sciendo 2015-12-01
Series:Nova Biotechnologica et Chimica
Subjects:
hCG
Online Access:http://www.degruyter.com/view/j/nbec.2015.14.issue-2/nbec-2015-0023/nbec-2015-0023.xml?format=INT
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spelling doaj-2321b2befa16458397bdbf5407a10f872020-11-25T01:33:14ZengSciendoNova Biotechnologica et Chimica1338-69052015-12-0114214115710.1515/nbec-2015-0023nbec-2015-0023Interaction Of Calcium Phosphate Nanoparticles With Human Chorionic Gonadotropin Modifies Secondary And Tertiary Protein StructureAl-Hakeim Hussein K0Al-Zabeba Rahman S.1Grulke Eric2Jaffar Al-Mulla Emad A.3Department of Chemistry, Faculty of Science, University of Kufa, P.O. Box 21, An-Najaf 54001, IraqDepartment of Chemistry, Faculty of Science, University of Kufa, P.O. Box 21, An-Najaf 54001, IraqDepartment of Chemical Engineering, College of Engineering, Kentucky University, USADepartment of Chemistry, Faculty of Science, University of Kufa, P.O. Box 21, An-Najaf 54001, IraqCalcium phosphate nanoparticles (CaPNP) have good biocompatibility and bioactivity inside human body. In this study, the interaction between CaPNP and human chorionic gonadotropin (hCG) was analyzed to determine the changes in the protein structure in the presence of CaPNP and the quantity of protein adsorbed on the CaPNP surface. The results showed a significant adsorption of hCG on the CaPNP nanoparticle surface. The optimal fit was achieved using the Sips isotherm equation with a maximum adsorption capacity of 68.23 µg/mg. The thermodynamic parameters, including ∆H° and ∆G°, of the adsorption process are positive, whereas ∆S° is negative. The circular dichroism results of the adsorption of hCG on CaPNP showed the changes in its secondary structure; such changes include the decomposition of α-helix strand and the increase in β-pleated sheet and random coil percentages. Fluorescence study indicated minimal changes in the tertiary structure near the microenvironment of the aromatic amino acids such as tyrosine and phenyl alanine caused by the interaction forces between the CaPNP and hCG protein. The desorption process showed that the quantity of the hCG desorbed significantly increases as temperature increases, which indicates the weak forces between hCG and the surface.http://www.degruyter.com/view/j/nbec.2015.14.issue-2/nbec-2015-0023/nbec-2015-0023.xml?format=INTCalcium phosphate nanoparticleshCGproteinsecondary structureand tertiary structure
collection DOAJ
language English
format Article
sources DOAJ
author Al-Hakeim Hussein K
Al-Zabeba Rahman S.
Grulke Eric
Jaffar Al-Mulla Emad A.
spellingShingle Al-Hakeim Hussein K
Al-Zabeba Rahman S.
Grulke Eric
Jaffar Al-Mulla Emad A.
Interaction Of Calcium Phosphate Nanoparticles With Human Chorionic Gonadotropin Modifies Secondary And Tertiary Protein Structure
Nova Biotechnologica et Chimica
Calcium phosphate nanoparticles
hCG
protein
secondary structure
and tertiary structure
author_facet Al-Hakeim Hussein K
Al-Zabeba Rahman S.
Grulke Eric
Jaffar Al-Mulla Emad A.
author_sort Al-Hakeim Hussein K
title Interaction Of Calcium Phosphate Nanoparticles With Human Chorionic Gonadotropin Modifies Secondary And Tertiary Protein Structure
title_short Interaction Of Calcium Phosphate Nanoparticles With Human Chorionic Gonadotropin Modifies Secondary And Tertiary Protein Structure
title_full Interaction Of Calcium Phosphate Nanoparticles With Human Chorionic Gonadotropin Modifies Secondary And Tertiary Protein Structure
title_fullStr Interaction Of Calcium Phosphate Nanoparticles With Human Chorionic Gonadotropin Modifies Secondary And Tertiary Protein Structure
title_full_unstemmed Interaction Of Calcium Phosphate Nanoparticles With Human Chorionic Gonadotropin Modifies Secondary And Tertiary Protein Structure
title_sort interaction of calcium phosphate nanoparticles with human chorionic gonadotropin modifies secondary and tertiary protein structure
publisher Sciendo
series Nova Biotechnologica et Chimica
issn 1338-6905
publishDate 2015-12-01
description Calcium phosphate nanoparticles (CaPNP) have good biocompatibility and bioactivity inside human body. In this study, the interaction between CaPNP and human chorionic gonadotropin (hCG) was analyzed to determine the changes in the protein structure in the presence of CaPNP and the quantity of protein adsorbed on the CaPNP surface. The results showed a significant adsorption of hCG on the CaPNP nanoparticle surface. The optimal fit was achieved using the Sips isotherm equation with a maximum adsorption capacity of 68.23 µg/mg. The thermodynamic parameters, including ∆H° and ∆G°, of the adsorption process are positive, whereas ∆S° is negative. The circular dichroism results of the adsorption of hCG on CaPNP showed the changes in its secondary structure; such changes include the decomposition of α-helix strand and the increase in β-pleated sheet and random coil percentages. Fluorescence study indicated minimal changes in the tertiary structure near the microenvironment of the aromatic amino acids such as tyrosine and phenyl alanine caused by the interaction forces between the CaPNP and hCG protein. The desorption process showed that the quantity of the hCG desorbed significantly increases as temperature increases, which indicates the weak forces between hCG and the surface.
topic Calcium phosphate nanoparticles
hCG
protein
secondary structure
and tertiary structure
url http://www.degruyter.com/view/j/nbec.2015.14.issue-2/nbec-2015-0023/nbec-2015-0023.xml?format=INT
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AT grulkeeric interactionofcalciumphosphatenanoparticleswithhumanchorionicgonadotropinmodifiessecondaryandtertiaryproteinstructure
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