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Serine Protease Inhibitors-New Molecules for Modification of Polymeric Biomaterials.
- Source :
-
Biomolecules [Biomolecules] 2020 Jan 04; Vol. 10 (1). Date of Electronic Publication: 2020 Jan 04. - Publication Year :
- 2020
-
Abstract
- Three serine protease inhibitors (AEBSF, soy inhibitor, α <subscript>1</subscript> -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 <subscript>1</subscript> -antitrypsin inhibited the adhesion and multiplication of Staphylococcus aureus subs. aureus ATCC <superscript>®</superscript> 25923 <superscript>TM</superscript> and Candida albicans 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.
- Subjects :
- Anti-Bacterial Agents pharmacology
Biocompatible Materials chemical synthesis
Biocompatible Materials pharmacology
Candida albicans drug effects
Endopeptidases
Humans
Polymers
Staphylococcus aureus drug effects
Sulfones chemistry
Sulfones pharmacology
alpha 1-Antitrypsin chemistry
alpha 1-Antitrypsin pharmacology
Serine Proteinase Inhibitors chemistry
Serine Proteinase Inhibitors metabolism
Serine Proteinase Inhibitors pharmacology
Subjects
Details
- Language :
- English
- ISSN :
- 2218-273X
- Volume :
- 10
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biomolecules
- Publication Type :
- Academic Journal
- Accession number :
- 31947983
- Full Text :
- https://doi.org/10.3390/biom10010082