Biology subjects

Kehribar, E. S.

Publications and source records attributed to Kehribar, E. S..

2 recordsLinked to original sources

bioRxiv2023

An Antibiotic Degrading Engineered Living Material Platform to Combat Environmental Antibiotic Resistance

Presence of antibiotics in natural water bodies is a growing problem regarding the occurrence of antibiotic resistance among various species. This is mainly caused due to excessive use of medical and veterinary antibiotics as well as the lack of effective treatment processes for eliminating residual antibiotic from wastewaters. In this study, we introduce a genetically engineered biomaterial as a solution for effective degradation of one of the dominantly found antibiotics in natural water bodies. Our biomaterial harnesses laccase type enzymes which are known to attack specific type of antibiotics, i.e. fluoroquinolone type synthetic antibiotics, and as a result degradation occurs. The engineered biomaterial is built using Escherichia coli biofilm protein CsgA as a scaffold, which is fused separately to two different laccase enzymes with the SpyTag - SpyCatcher peptide-protein duo. The final material is implemented as a part of a living material system. Our proposed system can be integrated as living antibiotic degrading materials to help the combat with antibiotic resistance.

synthetic biology↗

bioRxiv2020

Binding Behavior of Microbial Functional Amyloidson Solid Surfaces

Self-assembling protein subunits hold great potential as biomaterials with improved functions. Among the self-assembled protein structures functional amyloids are promising unique properties such as resistance to harsh physical and chemical conditions their mechanical strength, and ease of functionalization. Curli proteins, which are functional amyloids of bacterial biofilms can be programmed as intelligent biomaterials. In order to obtain controllable curli based biomaterials for biomedical applications, and to understand role of each of the curli forming monomeric proteins (namely CsgA and CsgB from Escherichia coli) we characterized their binding kinetics to gold, hydroxyapatite, and silica surfaces. We demonstrated that CsgA, CsgB, and their equimolar mixture have different binding strengths for different surfaces. On hydroxyapatite and silica surfaces, CsgB is the crucial element that determines the final adhesiveness of the CsgA-CsgB mixture. On the gold surface, on the other hand, CsgA controls the behavior of the mixture. Those findings uncover the binding behavior of curli proteins CsgA and CsgB on different biomedically valuable surfaces to obtain a more precise control on their adhesion to a targeted surface.

microbiology↗