Trans interactions between galactosylceramide and cerebroside sulfate across apposed bilayers.

The two glycosphingolipids galactosylceramide (GalC) and its sulfated form, cerebroside sulfate (CBS), are present at high concentrations in the multilayered myelin sheath and are involved in carbohydrate-carbohydrate interactions between the lipid headgroups. In order to study the structure of the complex of these two glycolipids by Fourier transform infrared (FTIR) spectroscopy, GalC dispersions were combined with CBS dispersions in the presence and absence of Ca(2+). The FTIR spectra indicated that a strong interaction occurred between these glycolipids even in the absence of Ca(2+). The interaction resulted in dehydration of the sulfate, changes in the intermolecular hydrogen bonding interactions of the sugar and other oxygens, decreased intermolecular hydrogen bonding of the amide C==O of GalC and dehydration of the amide region of one or both of the lipids in the mixture, and disordering of the hydrocarbon chains of both lipids. The spectra also show that Ca(2+) interacts with the sulfate of CBS. Although they do not reveal which other groups of CBS and GalC interact with Ca(2+) or which groups participate in the interaction between the two lipids, they do show that the sulfate is not directly involved in interaction with GalC, since it can still bind to Ca(2+) in the mixture. The interaction between these two lipids could be either a lateral cis interaction in the same bilayer or a trans interaction between apposed bilayers. The type of interaction between the lipids, cis or trans, was investigated using fluorescent and spin-label probes and anti-glycolipid antibodies. The results confirmed a strong interaction between the GalC and the CBS microstructures. They suggested further that this interaction caused the CBS microstructures to be disrupted so that CBS formed a single bilayer around the GalC multilayered microstructures, thus sequestering GalC from the external aqueous phase. Thus the CBS and GalC interacted via a trans interaction across apposed bilayers, which resulted in dehydration of the headgroup and interface region of both lipid bilayers. The strong interaction between these lipids may be involved in stabilization of the myelin sheath

Impurity-defect interaction in polycrystalline silicon for photovoltaic applications. The role of hydrogen

An overview of the studies done by the authors on the physicochemical behaviour of some impurities (P, C, H) in silicon is given. Results concern : diffusion and segregation of impurities in mono and polycrystalline silicon, passivation of recombining defects by hydrogen, hydrogen-dopant interaction. A more focused interest is given on hydrogen diffusion and behaviour. The results are discussed, taking into account the existence of complex mechanisms of interaction between hydrogen and impurities or defects.Cet article résume les études effectuées par les auteurs sur le comportement physico-chimique de quelques impuretés (P, C, H) dans le silicium. Les résultats portent sur : la diffusion et la ségrégation d'impuretés dans le silicium mono et polycristallin, la passivation des défauts recombinants par l'hydrogène, les interactions hydrogène-dopants. Un accent particulier est mis sur le comportement et la diffusion de l'hydrogène. Les résultats sont discutés en tenant compte de l'existence de mécanismes complexes d'interactions entre l'hydrogène et les impuretés ou les défauts

Label-free amplified bioaffinity detection using terahertz wave technology

A new affinity biosensor based on pulsed terahertz (THz) wave technology has been used to monitor binding between biotin and avidin molecules. Amplified detection of avidin-biotin binding is obtained on supported membranes composed of biotin layers on quartz surface, which is modified with octadecanol. Agarose particles are conjugated with avidin and then applied to biotin, which is already bound to the octadecanol quartz surface, the biotin binds to the conjugate rapidly and causes an enhancement of the THz difference signal between biotin and biotin-avidin complexes by a factor greater than eight fold when compared to the same sample without agarose beads. The technique was able to detect less than 10.3 ng/cm2 avidin, thus, giving the THz system a detection capability of sub-thin solid films better than ellipsometry and reflectometry techniques. Further improvement is underway using highly refractive beads together with appropriate surface chemistry. This newly developed method is being saliently optimized for future application, including the detection of DNA hybridization and ligand-analyte affinity binding

Amplification and modelling of bioaffinity detection with terahertz spectroscopy

© 2003 COPYRIGHT SPIE--The International Society for Optical Engineering. Downloading of the abstract is permitted for personal use only.A new bioaffinity sensor based on pulsed terahertz (THz) spectroscopy is able to sensitively detect the presence of ultra-thin bound biomolecular layers. The protein avidin and lipid biotin are noted for their very high binding affinity, and the ease for which they can be attached to residues with importance in many biosensing applications. We demonstrate the sensitivity of the pulsed THz spectrometer to thin avidin layers and to avidin amplified with micron-sized agarose beads. The experimental results can be simply modelled by considering transmission of the THz radiation at the thin film interfaces. We detect less than 10.3 ng/cm2 avidin, giving the THz system a detection capability of sub-thin solid films better than ellipsometry and reflectometry techniques

Ricin trafficking in plant and mammalian cells

Ricin is a heterodimeric plant protein that is potently toxic to mammalian and many other eukaryotic cells. It is synthesized and stored in the endosperm cells of maturing Ricinus communis seeds (castor beans). The ricin family has two major members, both, lectins, collectively known as Ricinus communis agglutinin ll (ricin) and Ricinus communis agglutinin l (RCA). These proteins are stored in vacuoles within the endosperm cells of mature Ricinus seeds and they are rapidly broken down by hydrolysis during the early stages of post-germinative growth. Both ricin and RCA traffic within the plant cell from their site of synthesis to the storage vacuoles, and when they intoxicate mammalian cells they traffic from outside the cell to their site of action. In this review we will consider both of these trafficking routes

Thermal Unfolding of the Pertussis Toxin S1 Subunit Facilitates Toxin Translocation to the Cytosol by the Mechanism of Endoplasmic Reticulum-Associated Degradation

Pertussis toxin (PT) moves from the host cell surface to the endoplasmic reticulum (ER) by retrograde vesicular transport. The catalytic PTS1 subunit dissociates from the rest of the toxin in the ER and then shifts to a disordered conformation which may trigger its export to the cytosol through the quality control mechanism of ER-associated degradation (ERAD). Functional roles for toxin instability and ERAD in PTS1 translocation have not been established. We addressed these issues with the use of a surface plasmon resonance system to quantify the cytosolic pool of PTS1 from intoxicated cells. Only 3% of surface-associated PTS1 reached the host cytosol after 3 h of toxin exposure. This represented, on average, 38,000 molecules of cytosolic PTS1 per cell. Cells treated with a proteasome inhibitor contained larger quantities of cytosolic PTS1. Stabilization of the dissociated PTS1 subunit with chemical chaperones inhibited toxin export to the cytosol and blocked PT intoxication. ERAD-defective cell lines likewise exhibited reduced quantities of cytosolic PTS1 and PT resistance. These observations identify the unfolding of dissociated PTS1 as a trigger for its ERAD-mediated translocation to the cytosol

Label-free bioaffinity detection using terahertz technology

© 2002 IOP PublishingWe report the first use of differential terahertz time-domain spectroscopy for bioaffinity sensing. Binding is observed by measuring the transmission of a thin layer of biotin bound to the sensor protein avidin. We demonstrate the THz wave transmission of a sub-micron-thick film and sensitivity to 0.1 µg cm−2 of biotin. These results point the way for a host of biosensor applications using T-rays, or pulsed far-infrared (FIR) radiation.Samuel P Mickan, Abdellah Menikh, Haibo Liu, Carmen A Mannella, Robert MacColl, Derek Abbott, Jesper Munch and X-C Zhan