Bioapatite ceramics produced from biogenic sources provide highly attractive materials for the preparation of artificial replacements since such materials are not only more easily accepted by living organisms, but bioapatite isolated from biowaste such as xenogeneous bones also provides a low-cost material. Nevertheless, the presence of organic compounds in the bioapatite may lead to a deterioration in its quality and may trigger an undesirable immune response. Therefore, procedures which ensure the elimination of organic compounds through bioapatite isolation are being subjected to intense investigation and the presence of remaining organic impurities is being determined through the application of various methods. Since current conclusions concerning the conditions suitable for the elimination of organic compounds remain ambiguous, we used the mass spectrometry-based proteomic approach in order to determine the presence of proteins or peptides in bioapatite samples treated under the most frequently employed conditions, i.e., the alkaline hydrothermal process and calcination at 500 °C. Since we also investigated the presence of proteins or peptides in treated bioapatite particles of differing sizes, we discovered that both calcination and the size of the bioapatite particles constitute the main factors influencing the presence of proteins or peptides in bioapatite. In fact, while intact proteins were detected even in calcinated bioapatite consisting of particles >250 µm, no proteins were detected in the same material consisting of particles <40 µm. Therefore, we recommend the use of powdered bioapatite for the preparation of artificial replacements since it is more effectively purified than apatite in the form of blocks. In addition, we observed that while alkaline hydrothermal treatment leads to the non-specific cleavage of proteins, it does not ensure the full degradation thereof.

Department of Biochemistry and Microbiology University of Chemistry and Technology Prague Technická 3 166 28 Prague 6 Czech Republic

Department of Composite and Carbon Materials Institute of Rock Structure and Mechanics The Czech Academy of Sciences 5 Holešovičkách 41 182 09 Prague Czech Republic

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Nat Protoc. 2008;3(9):1444-51 PubMed

Connect Tissue Res. 1996;33(4):275-82 PubMed

Biomed Mater. 2011 Jun;6(3):035003 PubMed

Calcif Tissue Res. 1973;12(1):73-90 PubMed

J Nanosci Nanotechnol. 2014 Jan;14(1):546-63 PubMed

Rapid Commun Mass Spectrom. 2009 Dec;23(23):3843-54 PubMed

Anal Biochem. 2008 Mar 15;374(2):325-34 PubMed

Mol Cell Proteomics. 2012 Mar;11(3):M111.013987 PubMed

J Proteomics. 2010 Aug 5;73(9):1740-6 PubMed

Mol Cell Proteomics. 2005 Sep;4(9):1265-72 PubMed

Materials (Basel). 2010 Oct 15;3(10):4761-4772 PubMed

Biomaterials. 2004 Mar;25(6):987-94 PubMed

Biomaterials. 1994 May;15(6):433-7 PubMed

Rapid Commun Mass Spectrom. 2004;18(17):1896-900 PubMed

J Ultrastruct Res. 1970 Sep;32(5):545-8 PubMed

J Biomed Mater Res. 2000;53(3):227-34 PubMed

J Inorg Biochem. 1997 Oct;68(1):45-51 PubMed

Biomaterials. 2004 Jan;25(2):229-38 PubMed

Nature. 2011 May 19;473(7347):337-42 PubMed

Mol Cell Proteomics. 2006 Jan;5(1):144-56 PubMed

Nature. 2009 Aug 6;460(7256):762-5 PubMed

Biomed Mater. 2018 Apr 11;13(4):041001 PubMed

J Biol Chem. 1951 Nov;193(1):265-75 PubMed