Bacterium-Sculpted Porphyrin-Protein-Iron Sulfide Clusters for Distinction and Inhibition of Staphylococcus aureus
Microbe-catalyzed surface modification is a promising method for the production of special targeting nanomaterials. A bacterium-selective material can be obtained by investigating the microbe-catalyzed mineralization of proteins. Herein, a novel method was fabricated for the biosynthesis of FeS-deco...
Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1999. - 38(2022), 34 vom: 30. Aug., Seite 10385-10391 |
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Weitere Verfasser: | , |
Format: | Online-Aufsatz |
Sprache: | English |
Veröffentlicht: |
2022
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Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Bacterial Proteins Ferric Compounds Ferrous Compounds Porphyrins Serum Albumin, Bovine 27432CM55Q ferrous sulfide TH5J4TUX6S |
Zusammenfassung: | Microbe-catalyzed surface modification is a promising method for the production of special targeting nanomaterials. A bacterium-selective material can be obtained by investigating the microbe-catalyzed mineralization of proteins. Herein, a novel method was fabricated for the biosynthesis of FeS-decorated porphyrin-protein clusters (P-CABE) via E. coli (Escherichia coli)-catalyzed bio-Fe(III) reduction and bio-sulfidation of porphyrin (P), caffeic acid (CA), and protein [bovine serum albumin (BSA)] assemblies. The assembly (P-CA@BSA) was identified by spectroscopic methods. Next, the P-CA@BSA assembly was transferred into FeS-decorated porphyrin-protein clusters (P-CA@BE) catalyzed by E. coli. There are partial β-folding proteins in P-CA@BE, which selectively recognize S. aureus (Staphylococcus aureus) and show different antibacterial properties against E. coli and S. aureus. Results demonstrate that the E. coli-catalyzed mineralization of the porphyrin-protein assembly is an effective method for the biosynthesis of S. aureus-sensitive metal-protein clusters |
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Beschreibung: | Date Completed 31.08.2022 Date Revised 13.10.2022 published: Print-Electronic Citation Status MEDLINE |
ISSN: | 1520-5827 |
DOI: | 10.1021/acs.langmuir.2c00964 |