ABSTRACT
Ultrastrong coupling of light and matter creates new opportunities to modify chemical reactions or develop novel nanoscale devices. One-dimensional Luttinger-liquid plasmons in metallic carbon nanotubes are long-lived excitations with extreme electromagnetic field confinement. They are promising candidates to realize strong or even ultrastrong coupling at infrared frequencies. We applied near-field polariton interferometry to examine the interaction between propagating Luttinger-liquid plasmons in individual carbon nanotubes and surface phonon polaritons of silica and hexagonal boron nitride. We extracted the dispersion relation of the hybrid Luttinger-liquid plasmon-phonon polaritons (LPPhPs) and explained the observed phenomena by the coupled harmonic oscillator model. The dispersion shows pronounced mode splitting, and the obtained value for the normalized coupling strength shows we reached the ultrastrong coupling regime with both native silica and hBN phonons. Our findings predict future applications to exploit the extraordinary properties of carbon nanotube plasmons, ranging from nanoscale plasmonic circuits to ultrasensitive molecular sensing.
ABSTRACT
Nickel nanoclusters grown inside single-walled carbon nanotubes (SWCNT) were studied by infrared scattering-type scanning near-field optical microscopy (s-SNOM). The metal clusters give high local contrast enhancement in near-field phase maps caused by the excitation of free charge carriers. The experimental results are supported by calculations using the finite dipole model, approximating the clusters with elliptical nanoparticles. Compared to magnetic force microscopy, s-SNOM appears much more sensitive to detect metal clusters inside carbon nanotubes. We estimate that these clusters contain fewer than ≈700 Ni atoms.
ABSTRACT
Mannan-binding lectin (MBL)-associated serine proteases, MASP-1 and MASP-2, have been thought to autoactivate when MBL/ficolin·MASP complexes bind to pathogens triggering the complement lectin pathway. Autoactivation of MASPs occurs in two steps: 1) zymogen autoactivation, when one proenzyme cleaves another proenzyme molecule of the same protease, and 2) autocatalytic activation, when the activated protease cleaves its own zymogen. Using recombinant catalytic fragments, we demonstrated that a stable proenzyme MASP-1 variant (R448Q) cleaved the inactive, catalytic site Ser-to-Ala variant (S646A). The autoactivation steps of MASP-1 were separately quantified using these mutants and the wild type enzyme. Analogous mutants were made for MASP-2, and rate constants of the autoactivation steps as well as the possible cross-activation steps between MASP-1 and MASP-2 were determined. Based on the rate constants, a kinetic model of lectin pathway activation was outlined. The zymogen autoactivation rate of MASP-1 is â¼3000-fold higher, and the autocatalytic activation of MASP-1 is about 140-fold faster than those of MASP-2. Moreover, both activated and proenzyme MASP-1 can effectively cleave proenzyme MASP-2. MASP-3, which does not autoactivate, is also cleaved by MASP-1 quite efficiently. The structure of the catalytic region of proenzyme MASP-1 R448Q was solved at 2.5 Å. Proenzyme MASP-1 R448Q readily cleaves synthetic substrates, and it is inhibited by a specific canonical inhibitor developed against active MASP-1, indicating that zymogen MASP-1 fluctuates between an inactive and an active-like conformation. The determined structure provides a feasible explanation for this phenomenon. In summary, autoactivation of MASP-1 is crucial for the activation of MBL/ficolin·MASP complexes, and in the proenzymic phase zymogen MASP-1 controls the process.
