No abstract

An instrumentation technique for real-time, in situ and real space observation of microphase separation was proposed for ultra-high molecular weight block copolymer thin films (1010 kg mol À1 , domain spacing of 180 nm) under high solvent vapor swelling conditions. This is made possible by a combination of a homebuilt chamber which is capable of supplying sufficient amount of vapor, and force-distance curve measurements which gives real-time swollen film thickness and allow active feedback for controlling the degree of swelling. We succeeded in monitoring the domain coarsening of perpendicular lamellar structures in polystyrene-block-poly(methyl methacrylate) thin films for eight hours via tapping mode imaging. During the annealing process, the thickness reached a maximum of 8.5 times that of the original film. The series of temporal real space topographic images obtained via this method allowed us to study, for the first time, the growth exponent of the correlation length under solvent vapor annealing. † Electronic supplementary information (ESI) available: Solvent vapor annealing using reectometry, selective swelling of PS and PMMA homopolymers in THF, USAXS measurement of bulk BCP phase-separated pellets, defect analysis of AFM topographic images, and morphology assignment by SEM. See

Understanding the properties of cell membranes is important in the fields of fundamental and applied biology.

Energy landscape illustration from the streptavidin–biotin binding dynamics observed in high temporal-resolution AFM.

We developed a method to identify proteins adsorbed on solid surfaces from a solution containing a complex mixture of proteins by using Matrix-Assisted Laser Desorption/Ionization-Time of Flight mass (MALDI-ToF mass) spectroscopy. In the method, we performed all procedures of peptide mass fingerprint method including denaturation, reduction, alkylation, digestion, and spotting of matrix on substrates. The method enabled us to avoid artifacts of pipetting that could induce changes in the composition. We also developed an algorithm to identify the adsorbed proteins. In this work, we demonstrate the identification of proteins adsorbed on self-assembled monolayers (SAMs). Our results show that the composition of proteins on the SAMs critically depends on the terminal groups of the molecules constituting the SAMs, indicating that the competitive adsorption of protein molecules is largely affected by protein-surface interaction. The method introduced here can provide vital information to clarify the mechanism underlying the responses of cells and tissues to biomaterials.