New uses for ALD : By applying standard metal oxide atomic layer deposition (ALD) to two types of porphyrins, site‐specific chemical infiltration of substrate molecules is achieved: Diethylzinc can diffuse into the interior of porphyrin supramolecular structures and induce metalation of the porphyrin molecules from the vapor phase. A=Ph, p‐HO3SC6H4.
Size tunable amphiphilic NPs composed of poly(γ‐PGA) and hydrophobic amino acids, such as Phe or Trp, were prepared. To prepare these size‐regulated NPs, γ‐PGA‐g‐Phe or γ‐PGA‐g‐Trp dissolved in DMSO was added to various concentrations of NaCl solution. The γ‐PGA‐Phe and γ‐PGA‐Trp formed monodispersed NPs, and the size of NPs can be easily controlled by NaCl concentration. The different‐sized NPs showed the same structure. The encapsulation of protein into the different‐sized NPs was successfully achieved and the size of protein‐encapsulated γ‐PGA‐Phe NPs was increased when protein was encapsulated.
Tip-enhanced Raman mapping (TERM) can be used to obtain chemical analysis of a sample with a topographical resolution down to 15 nm. A short review of this technique is given. Among other samples (e.g. carbon nanotubes and graphene), we recently measured a high resolution tip-enhanced Raman map of a polymer for the first time. Using TERM, the phase separation behaviour of a polymer blend (PMMA/SAN) was monitored. In the early, incomplete state of phase separation an interface width of ∼200 nm was measured. A spatial resolution in the tens of nm range could be achieved. 相似文献
Anti-lysozyme aptamers are found to preferentially bind to the edge of a tightly packed lysozyme pattern. Such edge-binding
is due to the better accessibility and flexibility of the edge lysozyme molecules. Kelvin probe force microscopy (KPFM) was
used to study the aptamer–lysozyme binding. Our results show that KPFM is capable of detecting the aptamer–protein binding
down to the 30 nm scale. The surface potential of the aptamer–lysozyme complex is approximately 12 mV lower than that of the
lysozyme. The surface potential images of the aptamer-bound lysozyme patterns have the characteristic shoulder steps around
the pattern edge, which is much wider than that of a clean lysozyme pattern. These results demonstrate the potentials of KPFM
as a label-free method for the detection of protein–DNA interactions.
Figure Aptamers preferentially bind on the edge of a protein pattern as revealed by Kelvin force microscopy.