RESUMO
Evaluating the potential of using both synthetic and biological products as targeting agents for the diagnosis, imaging, and treatment of infections due to particularly antibiotic-resistant pathogens is important for controlling infections. We examined the interaction between Gp45, a receptor-binding protein of the Ï11 lysogenic phage, and its host S. aureus, a common cause of nosocomial infections. Using molecular dynamics and docking simulations, we identified the peptides that bind to S. aureus wall teichoic acids via Gp45. We compared the binding affinity of Gp45 and the two highest-scoring peptide sequences (P1 and P3) and their scrambled forms using microscopy, spectroscopy, and ELISA. Our results revealed that rGp45 (recombinant Gp45) and chemically synthesized P1 had a higher binding affinity for S. aureus compared with all other peptides, with the exception of E. coli. Furthermore, rGp45 had a capture efficiency of over 86%; P1 had a capture efficiency of over 64%. Overall, our findings suggest that receptor-binding proteins such as rGp45, which provide a critical initiation of the phage life cycle for host adsorption, might play an important role in the diagnosis, imaging, and targeting of bacterial infections. Studying such proteins could accordingly enable the development of effective strategies for controlling infections.
RESUMO
Conventional wound dressings fail to provide features that can assist the healing process of chronic wounds. Multifunctional wound dressings address this issue by incorporating attributes including antibacterial and antioxidant activity, and the ability to enhance wound healing. Herein, polyethylene glycol (PEG)-based antibacterial hydrogel sponge dressings are prepared by a rapid and facile gas foaming method based on an acid chloride/alcohol reaction where tannic acid (TA) is included as a reactant to impart antibacterial efficacy as well as to enhance the mechanical properties of the samples. The results reveal that the TA-integrated sponges possess excellent antibacterial properties against both Escherichia coli and Staphylococcus aureus with approximately 6-8 log reduction in the microbial colony count after 6 h, indicating their high potential for management of infection-prone wounds. Compared to the control sample, TA incorporation increases the elastic modulus by twofold. As the samples also exhibit biocompatibility, antioxidant activity, and wound healing capacity, the novel TA-incorporated hydrogels can be an alternative to traditional wound dressings for wounds with low-to-moderate exudate.
RESUMO
The aim of this study is to improve the solubility, chemical stability, and in vitro biological activity of caffeic acid phenethyl ester (CAPE) by forming inclusion complexes with ß-cyclodextrin (ß-CD) and hydroxypropyl-ß-cyclodextrin (Hß-CD) using the solvent evaporation method. The CAPE contents of the produced complexes were determined, and the complexes with the highest CAPE contents were selected for further characterization. Detailed characterization of inclusion complexes was performed by using Fourier transform infrared spectroscopy (FT-IR), X-ray diffraction (XRD), scanning electron microscopy (SEM), and electrospray ionization-mass spectrometry (ESI-MS). pH and thermal stability studies showed that both selected inclusion complexes exhibited better stability compared to free CAPE. Moreover, their antimicrobial activities were evaluated against Escherichia coli (E. coli) and Staphylococcus aureus (S. aureus) for the first time. According to the broth dilution assay, complexes with the highest CAPE content (10C/ß-CD and 10C/Hß-CD) exhibited considerable growth inhibition effects against both bacteria, 31.25 µg/mL and 62.5 µg/mL, respectively; contrarily, this value for free CAPE was 500 µg/mL. Furthermore, it was determined that the in vitro antioxidant activity of the complexes increased by about two times compared to free CAPE.
RESUMO
Bacteriophages, which selectively infect bacteria, and phage-derived structures are considered promising agents for the diagnosis and treatment of bacterial infections due to the increasing antibiotic resistance. The binding of phages to their specific receptors on host bacteria is highly specific and irreversible, and therefore, the characterization of receptor-binding proteins(RBPs), which are key determinants of phage specificity, is crucial for the development of new diagnostic and therapeutic products. This study highlights the biotechnological potential of Gp144, an RBP located in the tail baseplate of bacteriophage K and responsible for adsorption of phageK to S. aureus. Once it was established that recombinant Gp144 (rGp144)is biocompatible and does not exhibit lytic effects on bacteria, its interaction with the host, the binding efficiency and performance were assessed in vitro using microscopic and serological methods. Results showed that rGp144 has a capture efficiency (CE) of over 87% and the best CE score is %96 which captured 9 CFU mL-1 out of 10 CFU mL-1 bacteria, indicating that very low number of bacteria could be detected. Additionally, it was shown for the first time in the literature that rGp144 binds to both S. aureus and methicillin-resistant S. aureus (MRSA) cells in vitro, while its affinity to different Gram-positive bacteria (E. faecalis and B. cereus) was not observed. The findings suggest that rGp144 can be effectively used for the diagnosis of S. aureus and MRSA, and that the use of RBPs in host-phage interaction can be a novel and effective strategy for imaging and diagnosing the site of infection.
