Field test of a continuous-variable quantum key distribution prototype

We have designed and realized a prototype that implements a continuous-variable quantum key distribution protocol based on coherent states and reverse reconciliation. The system uses time and polarization multiplexing for optimal transmission and detection of the signal and phase reference, and employs sophisticated error-correction codes for reconciliation. The security of the system is guaranteed against general coherent eavesdropping attacks. The performance of the prototype was tested over preinstalled optical fibres as part of a quantum cryptography network combining different quantum key distribution technologies. The stable and automatic operation of the prototype over 57 hours yielded an average secret key distribution rate of 8 kbit/s over a 3 dB loss optical fibre, including the key extraction process and all quantum and classical communication. This system is therefore ideal for securing communications in metropolitan size networks with high speed requirements.Comment: 15 pages, 6 figures, submitted to New Journal of Physics (Special issue on Quantum Cryptography

Feasibility of quantum key distribution through dense wavelength division multiplexing network

In this paper, we study the feasibility of conducting quantum key distribution (QKD) together with classical communication through the same optical fiber by employing dense-wavelength-division-multiplexing (DWDM) technology at telecom wavelength. The impact of the classical channels to the quantum channel has been investigated for both QKD based on single photon detection and QKD based on homodyne detection. Our studies show that the latter can tolerate a much higher level of contamination from the classical channels than the former. This is because the local oscillator used in the homodyne detector acts as a "mode selector" which can suppress noise photons effectively. We have performed simulations based on both the decoy BB84 QKD protocol and the Gaussian modulated coherent state (GMCS) QKD protocol. While the former cannot tolerate even one classical channel (with a power of 0dBm), the latter can be multiplexed with 38 classical channels (0dBm power each channel) and still has a secure distance around 10km. Preliminary experiment has been conducted based on a 100MHz bandwidth homodyne detector.Comment: 18 pages, 5 figure

Upregulation of α7 Nicotinic Receptors by Acetylcholinesterase C-Terminal Peptides

BACKGROUND: The alpha-7 nicotinic acetylcholine receptor (alpha7-nAChR) is well known as a potent calcium ionophore that, in the brain, has been implicated in excitotoxicity and hence in the underlying mechanisms of neurodegenerative disorders such as Alzheimer's disease. Previous research implied that the activity of this receptor may be modified by exposure to a peptide fragment derived from the C-terminal region of the enzyme acetylcholinesterase. This investigation was undertaken to determine if the functional changes observed could be attributed to peptide binding interaction with the alpha7-nAChR, or peptide modulation of receptor expression. METHODOLOGY/PRINCIPAL FINDINGS: This study provides evidence that two peptides derived from the C-terminus of acetylcholinesterase, not only selectively displace specific bungarotoxin binding at the alpha7-nAChR, but also alter receptor binding properties for its familiar ligands, including the alternative endogenous agonist choline. Of more long-term significance, these peptides also induce upregulation of alpha7-nAChR mRNA and protein expression, as well as enhancing receptor trafficking to the plasma membrane. CONCLUSIONS/SIGNIFICANCE: The results reported here demonstrate a hitherto unknown relationship between the alpha7-nAChR and the non-enzymatic functions of acetylcholinesterase, mediated independently by its C-terminal domain. Such an interaction may prove valuable as a pharmacological tool, prompting new approaches for understanding, and combating, the process of neurodegeneration

Upregulation of α7 Nicotinic Receptors by Acetylcholinesterase C-Terminal Peptides

BACKGROUND: The alpha-7 nicotinic acetylcholine receptor (alpha7-nAChR) is well known as a potent calcium ionophore that, in the brain, has been implicated in excitotoxicity and hence in the underlying mechanisms of neurodegenerative disorders such as Alzheimer's disease. Previous research implied that the activity of this receptor may be modified by exposure to a peptide fragment derived from the C-terminal region of the enzyme acetylcholinesterase. This investigation was undertaken to determine if the functional changes observed could be attributed to peptide binding interaction with the alpha7-nAChR, or peptide modulation of receptor expression. METHODOLOGY/PRINCIPAL FINDINGS: This study provides evidence that two peptides derived from the C-terminus of acetylcholinesterase, not only selectively displace specific bungarotoxin binding at the alpha7-nAChR, but also alter receptor binding properties for its familiar ligands, including the alternative endogenous agonist choline. Of more long-term significance, these peptides also induce upregulation of alpha7-nAChR mRNA and protein expression, as well as enhancing receptor trafficking to the plasma membrane. CONCLUSIONS/SIGNIFICANCE: The results reported here demonstrate a hitherto unknown relationship between the alpha7-nAChR and the non-enzymatic functions of acetylcholinesterase, mediated independently by its C-terminal domain. Such an interaction may prove valuable as a pharmacological tool, prompting new approaches for understanding, and combating, the process of neurodegeneration