Collagenase Activity of Bromelain Immobilized at Gold Nanoparticle Interfaces for Therapeutic Applications
| Autor: | Marcelo Y. Icimoto, Vitor Oliveira, Iseli L. Nantes-Cardoso, Adrianne M. M. Brito |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
collagen
Circular dichroism Proteases Pharmaceutical Science 02 engineering and technology Article law.invention 03 medical and health sciences Pharmacy and materia medica Confocal microscopy law cysteine protease Thermal stability Surface plasmon resonance 030304 developmental biology 0303 health sciences nanotechnology Chemistry bromelain 021001 nanoscience & nanotechnology Cysteine protease RS1-441 Membrane Colloidal gold gold nanoparticles Biophysics 0210 nano-technology |
| Zdroj: | Pharmaceutics, Vol 13, Iss 1143, p 1143 (2021) Pharmaceutics Volume 13 Issue 8 |
| ISSN: | 1999-4923 |
| Popis: | Bromelain (Bro) is a multiprotein complex extracted from the pineapple plant Ananas comosus, composed of at least eight cysteine proteases. Bro has a wide range of applications in medicine and industry, where the stability of its active proteases is always a major concern. The present study describes the improvement of stability and gain of specific activity in the enzymatic content of Bro immobilized on gold nanoparticles (GNPs). GNPs were synthesized in situ using Bro as the reducing and stabilizing agents and characterized by surface plasmon resonance and transmission electron microscopy. Consistent with the structural changes observed by circular dichroism analysis, the association with GNPs affected enzyme activity. The active Bro immobilized on GNPs (NanoBro) remained stable under storage and gained thermal stability consistent with a thermophilic enzyme. Proteolytic assays were performed on type I collagen membranes using fluorescence spectroscopy of O-phthaldialdehyde (OPA), changes in the membrane superficial structure, and topography by scanning electron microscopy, FTIR, and scanning laser confocal microscopy. Another characteristic of the NanoBro observed was the significant increase in susceptibility to the inhibitory effect of E-64, indicating a gain in cysteine protease activity. The higher stability and specific activity of NanoBro contributed to the broadening and improvement of Bro applications. |
| Databáze: | OpenAIRE |
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