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

Open access


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.

If the inline PDF is not rendering correctly, you can download the PDF file here.

  • ADAMCZYK Z. BARBASZ J.: CIEŚLA M. Mechanisms of fibrinogen adsorption at solid substrates. Langmuir 27 2011 6868 - 6878.

  • AHMED M.J. DHEDAN S.K.: Equilibrium isotherms and kinetics modeling of methylene blue adsorption on agricultural wastes-based activated carbons. Fluid Phase Equilib. 317 2012 317: 9-14.

  • AL-HAKEIM H.K. AL-DAHAN I.M. AL-HILLAWI Z.H. BUSTAN R.S.: Interaction of prolactin hormone with the surfaces of two new azo compounds. Int. J. Pharm. Pharm. Sci. 6 2014 383-387.

  • APTHORN A.J. HARRIS D.C. LITTLEJOHN A. LUSTBADER J.W. CANFIELD R.E. MACHIN K.J. MORGAN F.J. ISAACS N.W.: Crystal structure of human chorionic gonadotropin. Nature 369 1994 455-61.

  • BONEVICH J.E.: Preparation and properties of nanoparticles of calcium phosphates with various Ca/P ratios. J. Res. Nat. Inst. Stand. Technol. 115 2010 243-255.

  • CAMARERO J. KWON Y. COLEMAN M.: Chemoselective attachment of biologically active proteins to surfaces by expressed protein ligation and its application for “protein chip” fabrication. J. Am. Chem. Soc. 126 2004 14730-14731.

  • CAOL S.T. WANG X. LUO G.P. LIU J.H. SAHU S. LIU Y. SUN Y.P.: Competitive performance of carbon “Quantum” dots in optical bioimaging. Theranostics 2 2012 295-301.

  • CHANE-CHING J.Y. LEBUGLE A. ROUSSELOT I. POURPOINT A. PELLE F.: Colloidal synthesis and characterization of monocrystalline apatite nanophosphors. J. Mater. Chem. 17 2007 2904-2913.

  • CHAUDHURI S. CHAKRABORTY S. SENGUPTA P.K.: Probing the interactions of hemoglobin with antioxidant flavonoids via fluorescence spectroscopy and molecular modeling studies. Biophys. Chem. 154 2011 26-34.

  • COLE L.A.: New discoveries on the biology and detection of human chorionic gonadotropin. Reprod. Biol. Endocrinol. 7 2009 8-37.

  • CORRÊA D.H. Ramos C.H.: The use of circular dichroism spectroscopy to study protein folding form and function. Afr. J. Biochem. Res. 3 2009 164-173.

  • CZESLIK C. JACKLER G. ROYER C.: Driving forces for the adsorption of enzymes at the water/silica interface studied by total internal reflection fluorescence spectroscopy and optical reflectometry. Spectroscopy 16 2002 139-145.

  • DE M.: Engineering the Nanoparticle Surface for Protein Recognition and Applications. A PhD Dissertation in Chemistry University of Massachusetts Amherst 2009 46-47.

  • EMRE C. MEHMET S. FATIH A.: Immobilization of urease on copper chelated EC-Tribeads and reversible adsorption. Afr. J. Biotechnol. 10 2011 6590-6597.

  • EPPLE M. GANESAN K. HEUMANN R. KLESING J. KOVTUN A. NEUMANN S. SOKOLOVAA V.: Application of calcium phosphate nanoparticles in biomedicine. J. Mater. Chem. 20 2010 18-23.

  • FEI L. PERRETT S.: Effect of nanoparticles on protein folding and fibrillogenesis. Int. J. Mol. Sci. 10 2009 646-655.

  • FENOGLIO I. FUBINI B. GHIBAUDI E.M. TURCI F.: Multiple aspects of the interaction of biomacromolecules with inorganic surfaces. Adv. Drug. Deliv. Rev. 63 2011 1186-1209.

  • FINNEY E.E. FINKE R.G.: Nanocluster nucleation and growth kinetic and mechanistic studies: A review emphasizing transition-metal nanoclusters. J. Coll. Interface Sci. 317 2008 351-374.

  • GARDNER D. SHOBACK D.: Greenspan's basic and clinical endocrinology. Ninth Edition Mc Graw Hill Lange USA 2011 2-5.

  • GILIOLI A. CAVEJON M. QUADRI M.: C. hildmannianus peel for Protein Adsorption. Chem. Eng. Transac. 32 2013 1099-1104.

  • HOIDY W.H. AHMAD M.B. YUNUS W.M.Z.W. IBRAHIM N.A.B.: Chemical synthesis and characterization of palm oil-based difatty acyl thiourea. J. Oleo Sci. 59 229-233.

  • HOLGADO M. SANZA F.J. LÓPEZ A. LAVÍN Á. CASQUEL R. LAGUNA M.F.: Description of an advantageous optical label-free biosensing interferometric read-out method to measure biological species. Sensors 14 2014 3675-3689.

  • JACKSON M.: Molecular and Cellular Biophysics. Cambridge University Press: New York Humana Press Inc. Totowa NJ. 2006 261-275.

  • JIN L. ZENG X. LIU M. DENG Y. HE N.: Current progress in gene delivery technology based on chemical methods and nano-carriers. Theranostics 4 2014 240-255.

  • KHAN T. AMANI S. NAEEM A.: Glycation promotes the formation of genotoxic aggregates in glucose oxidase. Amino Acid. 43 2012 1311.

  • KUMAR P. RAMALINGAM S. SATHISHKUMAR K. KOREAN J.: Adsorption characteristics of methylene blue onto the N-succinyl-chitosan-g-polyacrylamide/attapulgite composite. Chem. Eng. 28 2011 149-155.

  • LIONG M. LU J. KOVOCHICH M. XIA T. RUEHM S.G. NEL A.E. TAMANOI F. ZINK J.I.: Multifunctional inorganic nanoparticles for imaging targeting and drug delivery. ACS Nano 2 2008 889-896.

  • LIU X. QIN D. CUI Y. CHEN L. LI H. CHEN Z. GAO L. LI Y. LIU J.: The effect of calcium phosphate nanoparticles on hormone production and apoptosis in human granulosa cells. Reprod. Biol. Endocrinol. 8 2010 32.

  • LUNDQVIST M. SETHSON I. JONSSON B.H.: Protein adsorption onto silica nanoparticles: Conformational changes depend on the particle’s curvature and the protein stability. Langmuir 20 2004 10639-10647.

  • MANSUR H.S. RODRIGO L.O. LOBATO Z.P. VASCONCELOS W.L. MANSUR E.S. MACHADO L.J.: Adsorption/Desorption behavior of bovine serum albumin and porcine insulin on chemically patterned porous gel networks. Adsorption 7 2001 105-116.

  • MILLER R. GRIGORIEV D.O. KRAGEL J. MAKIEVSKI A.V. MALDONADO-VALDERRAMA J. LESERC M.E. MICHEL A. FAINERMAND V.B. Experimental studies on the desorption of adsorbed proteins from liquid interfaces. Food Hydrocolloid 19 2005 479-483.

  • MOFFET R.C. HENN T. LASKIN A. GILLES M.K.: Automated chemical analysis of internally mixed aerosol particles using x-ray spectromicroscopy at the Carbon K-Edge. Anal. Chem. 82 2010 7906-7914.

  • MONEMTABARY S. SHARIATI M. JAHANSHAHI N.M. GHOREYSHI A.A.: Equilibrium and thermodynamic studies of methane adsorption on multi-walled carbon nanotube. Iran. J. Energ. Environ. Nanotech. 4 2013 17-23.

  • NEOGI P. WANG J.C.: Stability of two-dimensional growth of a packed body of proteins on a solid surface. Langmuir. 9 2011 5347-53.

  • PEREZ-IRATXETA C. ANDRADE-NAVARRO M.A.: K2D2: estimation of protein secondary structure from circular dichroism spectra. BMC Struct. Biol. 8 2008 25.

  • RANJBAR B. GILL P.: Circular dichroism techniques: biomolecular and nanostructural analyses- A review. Chem. Biol. Drug. Des. 74 2009 101-120.

  • ROY I. MITRA S. MAITRA A. MOZUMDAR S.: Calcium phosphate nanoparticles as novel non-viral vectors for targeted gene delivery. Int. J. Pharm. 250 2003 25-33.

  • SHEMETOV A.A. NABIEV I. SUKHANOVA A.: Molecular interaction of proteins and peptides with nanoparticles. ACS Nano 6 2012 4585-4602.

  • SHIRAZI N. RANJBAR B. KHAJEH K. TAHEREH T.: Structure–function analysis of a new bacterial lipase: Effect of local structure reorganization on lipase activity. Int. J. Biol. Macromol. 54 2013 180-185.

  • STENMAN U.H. HOTAKAINEN K. ALFTHAN H.: Gonadotropins in doping: pharmacological basis and detection of illicit use. J. Pharmacol. 154 2008 569-583.

  • TOK A.B. DONG Z.S. MERTENS S.F.L. PITA M. FERNANDEZ V.M. SCHIFFRIN D.J.: Functionalization of thioctic acid capped gold nanoparticles for specific immobilization of histidine-tagged proteins. J. Am. Chem. Soc. 127 2005 5689-5694.

  • UMOREN S. ETIM U. ISRAEL A.: Adsorption of methylene blue from industrial effluent using poly (vinyl alcohol). Mater. J. Environ. Sci. 4 2013 75-86.

  • VAN DER VEEN M. STUART M.C. NORDE W.: Spreading of proteins and its effect on adsorption and desorption kinetics. Coll. Surfaces B: Biointerfaces 54 2007 136-142.

  • WANG B. WUA P. YOKELB R.A. GRULKE E.A.: Influence of surface charge on lysozyme adsorption to ceria nanoparticles. Appl. Surf. Sci. 258 2012 5332-5341.

  • WU H. LUSTBADER J.W. LIU Y. CANFIELD R.E. HENDRICKSON W.A.: Structure of human chorionic gonadotropin at 2.6A resolution from MAD analysis of the selenomethionyl protein. Structure 2 1994 545-558.

  • ZAMANI M. PRABHAKARAN M.P. RAMAKRISHNA S.: Advances in drug delivery via electrospun and electrosprayed nanomaterials. Int. J. Nanomed. 8 2013 2997-3017.

  • ZHANG Y.Z. ZHOU B. LIU Y.X. ZHOU C.X. DING X.L. LIU Y.: Fluorescence study on the interaction of bovine serum albumin with paminoazobenzene. J. Fluoresc. 18 2008 109-118.

  • ZIN W.Y. IBRAHIM N.A.B. Rahman M.Z.A.: Difatty acyl urea from corn oil: Synthesis and characterization. J. Oleo Sci. 59 157-160

  • ZHAO W. FANG Y. ZHU Q. WANG Q. LIU M. HUANG X. SHEN J.: A novel glucose biosensor based on phosphonic acid-functionalized silica nanoparticles for sensitive detection of glucose in real samples. Electrochim. Acta. 89 2013 278-283.

Journal information
Impact Factor

CiteScore 2018: 0.68

SCImago Journal Rank (SJR) 2018: 0.173
Source Normalized Impact per Paper (SNIP) 2018: 0.288

All Time Past Year Past 30 Days
Abstract Views 0 0 0
Full Text Views 377 137 4
PDF Downloads 137 65 2