Interfacially Self-Assembled Mutifunctional Protein Thin Films for Accelerated Wound Healing.

The design of mutifunctional protein films for large-area spatially ordered arrays of functional components holds great promise in the field of biomedical applications. Herein, interfacial electrostatic self-assembly was employed to construct a large-scale protein thin film by inducing electrostatic interactions between three bovine serum albumin (BSA)-coated nanoclusters and cetyltrimethylammonium bromide (CTAB), leading to their spontaneous organization and uniform distribution at the oil-water interface. This protein film demonstrated excellent multienzyme functions, high antibacterial activity, and pH-responsive drug release capability. Therefore, it can accelerate the wound closure process through a synergistic effect that includes reducing local blood glucose levels, regulating cellular oxidative stress, eradicating bacteria, and promoting cell proliferation.

Recent advances in ß-cyclodextrin-based materials for chiral recognition.

In nature, enantiomers are pairs of chiral compounds, and have semblable chemical and physical properties but mostly show opposite biological effects when they enter an organism. Therefore, chiral recognition has a crucial research value in the fields of medicine, food, biochemistry, etc. Cyclodextrins (CDs) are produced by cyclodextrin glucosyltransferase in some species of bacillus on starch and include three main members α-, ß-, and γ-CD with six, seven and eight units of glucose, respectively. With a hydrophilic external cavity and a hydrophobic internal cavity, ß-CD can also combine with a variety of materials (e.g., graphene, nanoparticles, COFs, and OFETs) to enhance the chiral recognition of guest molecules in a chiral sensor. This review presents the progress of ß-CD modification with different materials for chiral recognition and describes in detail how different materials assist ß-CD in chiral recognition and improve the effect of ß-CD chiral discrimination.

Molecular Dynamic Simulations of Bromodomain and Extra-Terminal Protein 4 Bonded to Potent Inhibitors.

Bromodomain and extra-terminal domain (BET) subfamily is the most studied subfamily of bromodomain-containing proteins (BCPs) family which can modulate acetylation signal transduction and produce diverse physiological functions. Thus, the BET family can be treated as an alternative strategy for targeting androgen-receptor (AR)-driven cancers. In order to explore the effect of inhibitors binding to BRD4 (the most studied member of BET family), four 150 ns molecular dynamic simulations were performed (free BRD4, Cpd4-BRD4, Cpd9-BRD4 and Cpd19-BRD4). Docking studies showed that Cpd9 and Cpd19 were located at the active pocket, as well as Cpd4. Molecular dynamics (MD) simulations indicated that only Cpd19 binding to BRD4 can induce residue Trp81-Ala89 partly become α-helix during MD simulations. MM-GBSA calculations suggested that Cpd19 had the best binding effect with BRD4 followed by Cpd4 and Cpd9. Computational alanine scanning results indicated that mutations in Phe83 made the greatest effects in Cpd9-BRD4 and Cpd19-BRD4 complexes, showing that Phe83 may play crucial roles in Cpd9 and Cpd19 binding to BRD4. Our results can provide some useful clues for further BCPs family search.