The characterization of polymer-polymer interfaces is of great interest to understand the diffusion process and chemical interactions in polymeric multiphase systems. This study investigated the formation of the interface layer between polyamide (PA) and polypropylene (PP) and its dependency on the maleic anhydride (MAH) content in PP. New insights with a very high level of details on the formation of the interfacial layer are obtained by employing a special technique of atomic force microscopy (AFM) combined with infrared (IR) for chemical imaging at nanoscale spatial resolution. This enables the determination of the interface thickness and even the observation and visualization of the diffusion gradient across the PA/PP interface layer. Combined with classical investigation methods such as interfacial energy and rheology, the method of nano-IR spectroscopy represents a very powerful tool to obtain more insights and a deeper understanding of the interfacial phenomenon in multiphase polymeric systems.On the highly oriented pyrolytic graphite (HOPG) surface, a new porphyrin molecule MT-4 containing a porphine core with six alkyl chains and two carboxyl groups has been explored using scanning tunneling microscopy (STM) technology. Solvent and pyridine regulation have been proved to be two effective ways to control and tune the supramolecular structure of MT-4 at interfaces. Different high-resolution STM (HR-STM) images with highly ordered and closely packed arrangements were gained at the corresponding liquid-solid interface, including phenyl octane (PO), 1-heptanoic acid (HA), and 1-hexanol. Except for the solvent effect, introducing pyridine derivatives such as 4,4'-vinylenedipyridine (DPE) and 4,4'-((1E,1'E)-(2,5-bis(octyloxy)-1,4-phenylene) bis(ethene-2,1-diyl)) dipyridine (PEBP-C8) is also effective to modulate the self-assembly of MT-4. With careful analysis of the STM pictures and the density functional theory (DFT) computational exploration, we figured out the molecular model, interaction energies, and self-assembly mechanism of each system at the interface. This work provides a simple and effective approach for quickly building diverse nanoarchitectures by utilizing different noncovalent interactions. Meanwhile, it would give a perspective to regulate and control self-assembly arrays for devising novel molecular-based materials through more optimal strategies.Because of their distinctive mode of action in targeting bacterial cell membranes, antimicrobial peptides (AMPs) are increasingly regarded as a potential candidate for the development of novel antibiotics to combat the wide spread of bacterial resistance. https://www.selleckchem.com/products/abt-199.html To date, understanding of the exact molecular process by which AMPs act on the real bacterial envelope remains challenging. Simultaneously, the aggregated state of AMPs upon interaction with bacterial envelopes is still elusive. Previously, we have demonstrated that the potent antibacterial activity of a designed surfactant-like peptide Ac-A9K-NH2 benefited greatly from its high self-assembling ability and appropriate self-assembled morphologies and sizes. By using high-resolution atomic force microscopy, we here not only follow the variations of the Escherichia coli cell envelope in the presence of Ac-A9K-NH2 but also characterize the peptide aggregates on the bacterial surface as well as on the substrate surface. The results, together with those from fluorescence, zeta potential, circular dichroism, and scanning electron microscopy measurements, indicate that both the positively charged peptide monomers and self-assembled nanostructures can directly act on the negatively charged bacterial surface, followed by their insertion into the bacterial membrane, the formation of surface nanopores, and membrane lysis. The mechanism of Ac-A9K-NH2 against E. coli is thus consistent with the detergent-like mode of action. This work enhances our mechanistic understanding of the antibacterial behaviors of self-assembling peptides that will be valuable in exploring their biomedical applications.Wavy patterns are interesting geometric patterns and commonly seen in nature, such as serpentine streams or snake tracks in the sand. Although many efforts have been devoted to fabricating artificial wavy structures, it remains a great challenge to obtain wavy structures with controllable curvatures and desired functional properties. Here, we present an unprecedented approach to generate wavy polymer structures by annealing electrospun core-shell fibers on polymer films. Polystyrene (PS)/poly(methyl methacrylate) (PMMA) core-shell fibers, produced via the viscosity-induced phase separation in the electrospinning process, are annealed on PMMA films using vapors of acetic acid, a selective solvent for PMMA but not for PS. After the swollen PMMA chains of the PMMA shells are shed, the revealed PS cores start to buckle, driven by the elastic force from the strain release, forming the wavy structures. The degrees of the buckling, measured by the curvatures and the amplitudes of the wavy structures, are controlled by the annealing times. Furthermore, fluorescent properties are selectively introduced to the wavy structures using pyrene solutions or pyrene-containing vapors, demonstrating the potential application as fluorescent wavy materials.A sessile droplet of a complex fluid exhibits several stages of drying leading to the formation of a final pattern on the substrate. We report such pattern formation in dehydrating droplets of protein (BSA) and salts (MgCl2 and KCl) at various concentrations of the two components (protein and salts) as part of a parametric study for the understanding of complex patterns of dehydrating biofluid droplets (blood and urine), which will eventually be used for diagnosis of bladder cancer. The exact analysis of the biofluid patterns will require a rigorous parametric study; however, the current work provides an initial understanding of the effect of the basic components present in a biofluid droplet. Arrangement of the protein and the salts, due to evaporation, leads to the formation of some very distinctive final structures at the end of the droplet lifetime. Furthermore, these structures can be manipulated by varying the initial ratio of the two components in the solution. MgCl2 forms chains of crystals beyond a threshold initial concentration of protein (>3 wt %).