5 research outputs found
Optical bulk-boundary dichotomy in a quantum spin Hall insulator
The bulk-boundary correspondence is a key concept in topological quantum
materials. For instance, a quantum spin Hall insulator features a bulk
insulating gap with gapless helical boundary states protected by the underlying
Z2 topology. However, the bulk-boundary dichotomy and distinction are rarely
explored in optical experiments, which can provide unique information about
topological charge carriers beyond transport and electronic spectroscopy
techniques. Here, we utilize mid-infrared absorption micro-spectroscopy and
pump-probe micro-spectroscopy to elucidate the bulk-boundary optical responses
of Bi4Br4, a recently discovered room-temperature quantum spin Hall insulator.
Benefiting from the low energy of infrared photons and the high spatial
resolution, we unambiguously resolve a strong absorption from the boundary
states while the bulk absorption is suppressed by its insulating gap. Moreover,
the boundary absorption exhibits a strong polarization anisotropy, consistent
with the one-dimensional nature of the topological boundary states. Our
infrared pump-probe microscopy further measures a substantially increased
carrier lifetime for the boundary states, which reaches one nanosecond scale.
The nanosecond lifetime is about one to two orders longer than that of most
topological materials and can be attributed to the linear dispersion nature of
the helical boundary states. Our findings demonstrate the optical bulk-boundary
dichotomy in a topological material and provide a proof-of-principal
methodology for studying topological optoelectronics.Comment: 26 pages, 4 figure
Peptides Trap the Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Fusion Intermediate at Two Sites
Human immunodeficiency virus type 1 (HIV-1) entry into target cells requires folding of two heptad-repeat regions (N-HR and C-HR) of gp41 into a trimer of N-HR and C-HR hairpins, which brings viral and target cell membranes together to facilitate membrane fusion. Peptides corresponding to the N-HR and C-HR of gp41 are potent inhibitors of HIV infection. Here we report new findings on the mechanism of inhibition of a N-HR peptide and compare these data with inhibition by a C-HR peptide. Using intact envelope glycoprotein (Env) under fusogenic conditions, we show that the N-HR peptide preferentially binds receptor-activated Env and that CD4 binding is sufficient for triggering conformational changes that allow the peptide to bind Env, results similar to those seen with the C-HR peptide. However, activation by both CD4 and chemokine receptors further enhances Env binding by both peptides. We also show that a nonconservative mutation in the N-HR of gp41 abolishes C-HR peptide but not N-HR peptide binding to gp41. These results indicate that there are two distinct sites in receptor-activated Env that are potential targets for drug or vaccine development
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