Serine Protease Inhibitors—New Molecules for Modification of Polymeric Biomaterials

Abstract

Three serine protease inhibitors (AEBSF, soy inhibitor, α1-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 α1-antitrypsin inhibited the adhesion and multiplication of Staphylococcus aureus subs. aureus ATCC® 25923TM 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.

Levels of SERPIN family proteins in peri‐implant crevicular fluid in patients with peri‐implantitis

“…Serine protease inhibitors (SERPINs), a superfamily of protease inhibitors, are responsible for lots of regulated processes such as coagulation, fibrinolysis, and inflammation 8,9 . SERPINs are important elements in regulating proteolytic pathways, controlling serine activity and preventing from excessive proteolysis 10 . More than 1500 members of SERPINs have been recorded till now and they exist in vertebrates, invertebrates, plants, bacteria 11 .…”

“…More than 1500 members of SERPINs have been recorded till now and they exist in vertebrates, invertebrates, plants, bacteria 11 . Vertebrates SERPINs, with distinct exon‐intron patterns, are classified into nine clades (A‐I) 10,12 …”

“…8,9 SERPINs are important elements in regulating proteolytic pathways, controlling serine activity and preventing from excessive proteolysis. 10 More than 1500 members of SERPINs have been recorded till now and they exist in vertebrates, invertebrates, plants, bacteria. 11 Vertebrates SERPINs, with distinct exon-intron patterns, are classified into nine clades (A-I).…”

“…11 Vertebrates SERPINs, with distinct exon-intron patterns, are classified into nine clades (A-I). 10,12 At present, the extension of clade B SERPINs (SERPINBs) has been a vast catalog of functions in primarily mammals and animals due to the chain of duplication events. Subsequently in human 18q21.3 chromosome location, the newest duplicates of SERPINB3 and SERPINB4.…”

Novel Targets and Therapeutic Strategies for Promoting Organ Repair and Regeneration

“…In addition, despite the use of antibiotics to modify prostheses, implant-associated infections still remain challenging due to the development of bacterial resistance. To address this issue, Szałapata et al examined the prospect of serine protease inhibitors (PIs), immobilized on prosthetic surfaces widely used in regenerative medicine, to prevent bacterial growth [27]. Initially, they monitored the activity of the PIs at different concentrations, pH values, and temperatures along with the concentration of cross-linker to establish the conditions for surface immobilization.…”