No abstract

We report a method to establish experimental conditions for tip-enhanced Raman spectroscopy (TERS) with low thermal and mechanical damage to samples. In this method, we monitor the thermal desorption of thiol molecules from a gold-coated probe of an atomic force microscope (AFM) via TERS spectra. Temperatures for desorption of thiol molecules (60-100 °C) from gold surfaces cover the temperature range for degradation of heat-sensitive biomaterials (e.g. proteins). By monitoring the desorption of the thiols on the probe, we can estimate the power of an excitation laser for the samples to reach their critical temperatures for thermal degradation. Furthermore, we also found that an active oscillation of AFM cantilevers significantly promotes the heat transfer from the probe to the surrounding medium. This enables us to employ a higher power density of the excitation laser, resulting in a stronger Raman signal compared with the signal obtained with a contact mode. We propose that this combinatory method is effective in acquiring strong TERS signals while suppressing thermal and mechanical damage to soft and heat-sensitive samples.

We report that the thermal stability of self-assembled monolayers (SAMs) of two isocyanide derivatives (1pentyl isocyanide and benzyl isocyanide) on a gold surface was drastically improved by their preparation at high temperature (373 K). In the case of conventionally prepared isocyanide SAMs, thermal desorption spectroscopy revealed that the isocyanides changed their adsorption states with corresponding increase in binding energy. The results of surface-enhanced Raman scattering spectroscopy measurements also clearly indicated the change in adsorption states at 373 K during heating. Theoretical calculations using density functional theory revealed that there are two stable adsorption states (atop and adatom configurations) and that the calculated vibrational energies are in good agreement with those observed in Raman spectra.

Peptide coatings on material surfaces have demonstrated wide application across materials science and biotechnology, facilitating the development of nanobio interfaces through surface modification. A guiding motivation in the field is to engineer peptides with a high and selective binding affinity to target materials. Herein, we introduce a quantitative force mapping method in order to evaluate the binding affinity of peptides to various hydrophilic oxide materials by atomic force microscopy (AFM). Statistical analysis of adhesion forces and probabilities obtained on substrates with a materials contrast enabled us to simultaneously compare the peptide binding affinity to different materials. On the basis of the experimental results and corresponding theoretical analysis, we discuss the role of various interfacial forces in modulating the strength of peptide attachment to hydrophilic oxide solid supports as well as to gold. The results emphasize the precision and robustness of our approach to evaluating the adhesion strength of peptides to solid supports, thereby offering guidelines to improve the design and fabrication of peptide-coated materials.

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