Surface wrinkles are commonly observed in large-scale of graphene films. As a new feature, the wrinkled surface of graphene films may directly affect bacterial viability by means of various interactions of bacterial cells with graphene sheets. In the present study, we introduce a wrinkled surface geometry of graphene oxide (GO) thin films for antibacterial application. Highly wrinkled GO films were formed by vacuum filtration of a GO suspension through a prestrained filter. Several types of wrinkled GO surfaces were obtained with different roughness grades determined by root-mean-square values. Antibacterial activity of the fabricated GO films toward three different bacterial species, Escherichia coli, Mycobacterium smegmatis, and Staphylococcus aureus, was evaluated in relation to surface roughness. Because of their nanoscopically corrugated nature, the wrinkled GO films exhibited excellent antibacterial properties. On the basis of our detailed observations, we propose a novel concept of the surrounded contact-based mechanism for antimicrobial activity of wrinkled GO films. It postulates formation of a mechanically robust GO surface "trap" that prompts interaction of bacteria with the diameter-matched GO sink, which results in substantial damages to the bacterial cell membrane. We believe that our approach uncovered a novel use of a promising two-dimensional material for highly effective antibacterial treatment.
The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect cells from stresses. HSP protein families are classified based on their molecular weights, mainly including large HSPs, HSP90, HSP70, HSP60, HSP40, and small HSPs. They function as molecular chaperons in cells and work as an integrated network, participating in the folding of newly synthesized polypeptides, refolding metastable proteins, protein complex assembly, dissociating protein aggregate dissociation, and the degradation of misfolded proteins. In addition to their chaperone functions, they also play important roles in cell signaling transduction, cell cycle, and apoptosis regulation. Therefore, malfunction of HSPs is related with many diseases, including cancers, neurodegeneration, and other diseases. In this review, we describe the current understandings about the molecular mechanisms of the major HSP families including HSP90/HSP70/HSP60/HSP110 and small HSPs, how the HSPs keep the protein proteostasis and response to stresses, and we also discuss their roles in diseases and the recent exploration of HSP related therapy and diagnosis to modulate diseases. These research advances offer new prospects of HSPs as potential targets for therapeutic intervention.
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