Serine Protease Inhibitors—New Molecules for Modification of Polymeric Biomaterials
Three serine protease inhibitors (AEBSF, soy inhibitor, α<sub>1</sub>-antitrypsin) were covalently immobilized on the surface of three polymer prostheses with the optimized method. The immobilization efficiency ranged from 11 to 51%, depending on the chosen inhibitor and biomate...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-01-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/10/1/82 |
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| author | Katarzyna Szałapata Monika Osińska-Jaroszuk Justyna Kapral-Piotrowska Bożena Pawlikowska-Pawlęga Rafał Łopucki Robert Mroczka Anna Jarosz-Wilkołazka |
| author_facet | Katarzyna Szałapata Monika Osińska-Jaroszuk Justyna Kapral-Piotrowska Bożena Pawlikowska-Pawlęga Rafał Łopucki Robert Mroczka Anna Jarosz-Wilkołazka |
| author_sort | Katarzyna Szałapata |
| collection | DOAJ |
| description | Three serine protease inhibitors (AEBSF, soy inhibitor, α<sub>1</sub>-antitrypsin) were covalently immobilized on the surface of three polymer prostheses with the optimized method. The immobilization efficiency ranged from 11 to 51%, depending on the chosen inhibitor and biomaterial. The highest activity for all inhibitors was observed in the case of immobilization on the surface of the polyester Uni-Graft prosthesis, and the preparations obtained showed high stability in the environment with different pH and temperature values. Modification of the Uni-Graft prosthesis surface with the synthetic AEBSF inhibitor and human α<sub>1</sub>-antitrypsin inhibited the adhesion and multiplication of <i>Staphylococcus aureus</i> subs. <i>aureus ATCC<sup>®</sup> 25923<sup>TM</sup></i> and <i>Candida albicans</i> from the collection of the Department of Genetics and Microbiology, UMCS. Optical profilometry analysis indicated that, after the immobilization process on the surface of AEBSF-modified Uni-Graft prostheses, there were more structures with a high number of protrusions, while the introduction of modifications with a protein inhibitor led to the smoothing of their surface. |
| first_indexed | 2024-12-10T05:05:48Z |
| format | Article |
| id | doaj.art-0c0aa89abbe44f569cfb2b2deb966133 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-12-10T05:05:48Z |
| publishDate | 2020-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-0c0aa89abbe44f569cfb2b2deb9661332022-12-22T02:01:14ZengMDPI AGBiomolecules2218-273X2020-01-011018210.3390/biom10010082biom10010082Serine Protease Inhibitors—New Molecules for Modification of Polymeric BiomaterialsKatarzyna Szałapata0Monika Osińska-Jaroszuk1Justyna Kapral-Piotrowska2Bożena Pawlikowska-Pawlęga3Rafał Łopucki4Robert Mroczka5Anna Jarosz-Wilkołazka6Department of Biochemistry and Biotechnology, Maria Curie-Skłodowska University, Akademicka 19, 20-033 Lublin, PolandDepartment of Biochemistry and Biotechnology, Maria Curie-Skłodowska University, Akademicka 19, 20-033 Lublin, PolandDepartment of Functional Anatomy and Cytobiology, Maria Curie-Skłodowska University, Akademicka 19, 20-033 Lublin, PolandDepartment of Functional Anatomy and Cytobiology, Maria Curie-Skłodowska University, Akademicka 19, 20-033 Lublin, PolandLaboratory of X-Ray Optics, Centre of Interdisciplinary Research, The John Paul II Catholic University of Lublin, Konstantynów 1, 20-708 Lublin, PolandLaboratory of X-Ray Optics, Centre of Interdisciplinary Research, The John Paul II Catholic University of Lublin, Konstantynów 1, 20-708 Lublin, PolandDepartment of Biochemistry and Biotechnology, Maria Curie-Skłodowska University, Akademicka 19, 20-033 Lublin, PolandThree serine protease inhibitors (AEBSF, soy inhibitor, α<sub>1</sub>-antitrypsin) were covalently immobilized on the surface of three polymer prostheses with the optimized method. The immobilization efficiency ranged from 11 to 51%, depending on the chosen inhibitor and biomaterial. The highest activity for all inhibitors was observed in the case of immobilization on the surface of the polyester Uni-Graft prosthesis, and the preparations obtained showed high stability in the environment with different pH and temperature values. Modification of the Uni-Graft prosthesis surface with the synthetic AEBSF inhibitor and human α<sub>1</sub>-antitrypsin inhibited the adhesion and multiplication of <i>Staphylococcus aureus</i> subs. <i>aureus ATCC<sup>®</sup> 25923<sup>TM</sup></i> and <i>Candida albicans</i> from the collection of the Department of Genetics and Microbiology, UMCS. Optical profilometry analysis indicated that, after the immobilization process on the surface of AEBSF-modified Uni-Graft prostheses, there were more structures with a high number of protrusions, while the introduction of modifications with a protein inhibitor led to the smoothing of their surface.https://www.mdpi.com/2218-273X/10/1/82covalent immobilizationprotease inhibitorsmodification of biomaterials |
| spellingShingle | Katarzyna Szałapata Monika Osińska-Jaroszuk Justyna Kapral-Piotrowska Bożena Pawlikowska-Pawlęga Rafał Łopucki Robert Mroczka Anna Jarosz-Wilkołazka Serine Protease Inhibitors—New Molecules for Modification of Polymeric Biomaterials Biomolecules covalent immobilization protease inhibitors modification of biomaterials |
| title | Serine Protease Inhibitors—New Molecules for Modification of Polymeric Biomaterials |
| title_full | Serine Protease Inhibitors—New Molecules for Modification of Polymeric Biomaterials |
| title_fullStr | Serine Protease Inhibitors—New Molecules for Modification of Polymeric Biomaterials |
| title_full_unstemmed | Serine Protease Inhibitors—New Molecules for Modification of Polymeric Biomaterials |
| title_short | Serine Protease Inhibitors—New Molecules for Modification of Polymeric Biomaterials |
| title_sort | serine protease inhibitors new molecules for modification of polymeric biomaterials |
| topic | covalent immobilization protease inhibitors modification of biomaterials |
| url | https://www.mdpi.com/2218-273X/10/1/82 |
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