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- Edqvist, Erik, 1975-
(författare)
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Applications of active materials
- 2009
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Doktorsavhandling (övrigt vetenskapligt/konstnärligt)abstract
- Energy efficiency is a vital key component when designing and miniaturizing self sustained microsystems. The smaller the system, the smaller is the possibility to store enough stored energy for a long and continuous operational time. To move such a system in an energy efficient way, a piezoelectrical locomotion module consisting of four resonating cantilevers has been designed, manufactured and evaluated in this work. The combination of a suitable substrate, a multilayered piezoelectric material to reduce the voltage, and a resonating drive mechanism resulted in a low power demand. A manufacturing process for multilayer cantilever actuators made of P(VDF-TrFE) with aluminum electrodes on a substrate of flexible printed circuit board (FPC), has been developed. An important step in this process was the development of an etch recipe for dry etching the multilayer actuators in an inductive plasma equipment. Formulas for the quasi static tip deflection and resonance frequency of a multilayered cantilever, have been derived. Through theses, it was found that the multilayered structures should be deposited on the polymer side of the FPC in order to maximize the tip deflection. Both a large and a miniaturized locomotion module were manufactured and connected by wires to verify that the three legged motion principal worked to move the structures forward and backward, and turn it right and left. By touching and adding load, to a fourth miniaturized cantilever, its ability to act as a contact sensor and carry object was verified. The presented locomotion module is part of a multifunctional microsystem, intended to be energy efficient and powered by a solar panel with a total volume of less than 25 mm3 and weight 65 mg. The whole system, consisting of a solar cell, an infra red communication module, an integrated circuit for control, three capacitors for power regulating, the locomotion module and an FPC connecting the different modules, was surface mounted using a state of the art industrial facility. Two fully assembled systems could be programmed both through a test connector and through optical sensors in the multifunctional solar cell. One of these was folded together to the final configuration of a robot. However, the entire system could not be tested under full autonomous operating conditions. On the other hand, using wires, the locomotion module could be operated and used to move the entire system from a peak-to-peak voltage of 3.0 V.
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| 2. |
- Henningsson, Susanne, 1977, et al.
(författare)
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Genetic Variation in Brain-Derived Neurotrophic Factor Is Associated with Serotonin Transporter but Not Serotonin-1A Receptor Availability in Men
- 2009
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Ingår i: Biological Psychiatry. - : Elsevier BV. - 0006-3223 .- 1873-2402. ; 66:5, s. 477-485
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Tidskriftsartikel (refereegranskat)abstract
- Background: The serotonergic system, including the serotonin transporter (5-HTT), which is the target of many antidepressants, seems to be influenced by brain-derived neurotrophic factor (BDNF). Methods: Positron emission tomography (PET) was used to address, in 25 and 53 healthy volunteers, respectively, the possible association between six polymorphisms in the gene encoding BDNF and the availability of two proteins expressed by serotonergic neurons: the 5-HTT, measured with the radioligand [C-11]MADAM, and the serotonin-1A (5-HT1A) receptor, measured with [C-11]WAY-100635. Results: Several single nucleotide polymorphisms were associated with [C-11]MADAM binding potential (BP) in most brain regions, male carriers of the valine/valine genotype of the Val66Met polymorphism displaying higher availability. Effect sizes ranged from a 50% to a threefold increase. In contrast, there was no association for [C-11]WAY-100635 BP. The observation that BDNF polymorphisms were associated with 5-HTT availability could be partly replicated in an independent population comprising nine male suicide attempters and nine matched control subjects, in which transporter availability had been measured with single photon emission computed tomography with I-123-beta-CIT as ligand. Conclusions: Our results suggest that genetic variation in BDNF influences 5-HTT but not 5-HT1A receptor density in the human brain.
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| 3. |
- Lundberg, Erik, 1975-
(författare)
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Transthyretin and the transthyretin-related protein: A structural study
- 2006
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Doktorsavhandling (övrigt vetenskapligt/konstnärligt)abstract
- Transthyretin (TTR) is one of several proteins involved in amyloid disease in humans. Unknown conformational changes of the native state of TTR result in aggregation of TTR molecules into amyloid fibrils, which accumulate in extracellular tissues. This may result in different clinical symptoms, e.g. polyneuropathy or cardiomyopathy, depending on their site of accumulation. Our long-term goal is to identify structural changes associated with amyloid formation. For this work, structural characterization of TTR from other species than human may provide valuable information. The three-dimensional X-ray crystallographic structure of TTR from sea bream (Sparus aurata) was determined at 1.75 Å resolution. Human and sea bream TTR were found to be structurally very similar. However, interesting differences were present in the area at and around -strand D, which in fish forms an extended loop region. Interestingly, this area is believed to dissociate from the structure prior to amyloid formation, to allow -strands A and B to participate in polymerization. During evolution, TTR from different species have developed differences in preference to their natural ligands, the thyroid hormones 3,5,3’-triiodo-L-thyronine (T3) and 3,5,3’,5’-tetraiodo-L-thyronine (T4). While human TTR has higher affinity for T4, the opposite is true in lower vertebrates, e.g. fish and reptiles. We have determined two separate structures of sea bream TTR in complex with T3 and T4, both at 1.9 Å resolution. A significantly wider entrance and narrower thyroid hormone binding channel provide a structural explanation to the differences in thyroid hormone preference between human and piscine TTR. In a separate work, we identified a novel protein family with structural similarity to TTR, which we named the transthyretin-related protein (TRP) family. To attain information about this protein family, we cloned, expressed, purified and characterized TRP from Escherichia coli (EcTRP). Furthermore, we solved the structure of EcTRP to 1.65 Å resolution. As predicted, EcTRP and human TTR are structurally very similar. Interesting structural differences are found in the area corresponding to the thyroid hormone binding site in TTR, which due to its amino acid conservation within the TRP family we identified as a putative ligand-binding site in TRPs. The function of the TRP is not known, however, recent studies suggest that it might be involved in purine catabolism. It has been shown that partial acid denaturation of human TTR results in amyloid-fibril formation. Interestingly, we have shown that sea bream TTR also forms amyloid-like fibrils in vitro, even though it shares only 52% sequence identity to human TTR. Corresponding studies on EcTRP did not generate amyloid-like fibrils. EcTRP has 30% sequence identity to human TTR. The fact that two of the proteins form amyloid fibrils and one does not means that they can serve as a model system for the study of amyloid formation. Further studies on these three proteins are currently performed to attain more information about the mechanism of amyloid formation.
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