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High-affinity Protease-resistant Analog Of Insulin-like Growth Factor Binding Protein-2: Potential Cancer Co-Therapeutic
Funder
National Health and Medical Research Council
Funding Amount
$294,423.00
Summary
In many human cancers, including prostate and breast cancer, serum levels of insulin-like growth factor (IGF)-II are elevated, and this growth factor has been strongly implicated in promoting the progression of these tumours. The action of IGF-II in stimulating tumour growth is mediated through Type 1 IGF receptors on the surface of the cells. The IGF binding protein, IGFBP-2, has been shown to increase the action of IGF-II in some cancer cells in vitro. by binding to the outside of the cells as ....In many human cancers, including prostate and breast cancer, serum levels of insulin-like growth factor (IGF)-II are elevated, and this growth factor has been strongly implicated in promoting the progression of these tumours. The action of IGF-II in stimulating tumour growth is mediated through Type 1 IGF receptors on the surface of the cells. The IGF binding protein, IGFBP-2, has been shown to increase the action of IGF-II in some cancer cells in vitro. by binding to the outside of the cells as an IGF-II-IGFBP-2 complex and then presenting the IGF-II to the receptor by a process of sustained release. We propose to produce a very high affinity form of insulin-like growth factor binding protein-2 (OOptimised IGFBP-2O) which will sequester the IGF-II and effectively prevent it from binding to the receptor or the native IGFBP-2. We shall also engineer the OOptimised IGFBP-2O so that it is unable to bind to the outside of the cells. With this novel peptide, OOptimised IGFBP-2O, we will test the hypothesis that the growth of insulin-like growth factor (IGF)-dependent tumours can be arrested by preventing the localisation and presentation of IGF-II to IGF receptors. We expect that the availability of such a sequestering agent for IGF-II will increase the effectiveness of current cancer chemotherapy agents since it is known that IGF-II can help save cancer cells from chemotherapy-induced death.Read moreRead less
Structural And Functional Studies On RNA Nuclear Retention Mediated By Paraspeckles: A Novel Gene Regulation
Funder
National Health and Medical Research Council
Funding Amount
$290,978.00
Summary
Dynamic interactions between proteins and nucleic acids are essential process in gene regulation, where aberrant regulation leads to various diseases including cancers. The project aims to examine the interactions between paraspeckle proteins and nucleic acid molecules via determination of the structures of protein-nucleic acid complexes at the atomic level. The results will provide a better understanding of a recently discovered gene regulation mechanism and a basis for new gene therapy.
Probing The Structure, Mechanism And Inhibition Of Indoleamine 2,3-Dioxygenase Using Structure- And Ligand-Based Studies
Funder
National Health and Medical Research Council
Funding Amount
$319,650.00
Summary
The human enzyme indoleamine 2,3-dioxygenase (IDO) is responsible for the initiation of a major enzymatic pathway, known as the kynurenine pathway. During certain immune and infectious diseases IDO becomes over-active and this leads to accumulation of neurotoxic kynurenine pathway compounds (metabolites). The elevated levels of these metabolites have been linked to severe mental deterioration associated with diseases such as AIDS (AIDS dementia complex), malaria and Alzheimer's disease. Several ....The human enzyme indoleamine 2,3-dioxygenase (IDO) is responsible for the initiation of a major enzymatic pathway, known as the kynurenine pathway. During certain immune and infectious diseases IDO becomes over-active and this leads to accumulation of neurotoxic kynurenine pathway compounds (metabolites). The elevated levels of these metabolites have been linked to severe mental deterioration associated with diseases such as AIDS (AIDS dementia complex), malaria and Alzheimer's disease. Several kynurenine pathway metabolites have also been linked to age-related nuclear cataract, which is the major cause of human blindness. This project employs a multidisciplinary approach that brings together a team of expert scientists from medicinal chemistry, protein crystallography, protein biochemistry and neurology. The overall aims of the project are to determine the structure of IDO using the recombinant human enzyme that we have cloned and expressed in an active form and to develop compounds that will regulate levels of the kynurenine pathway metabolites by selectively inhibiting the action of IDO. In addition, we will begin to assess the medicinal value of the best inhibitors. We have already synthesised several inhibitors of IDO, but wish to design more potent inhibitors. In order to do this, computer-aided molecular modelling and X-ray crystallography (which effectively provides a picture of the enzyme with the inhibitors attached) will be used to predict the best molecular features needed for inhibition. This will greatly aid the design of new inhibitor compounds, which will then be synthesised. The best inhibitors will also be examined to determine their general pharmacological value and specifically their ability to treat AIDS dementia complex and age-related nuclear cataract. These enzyme inhibitors also have the potential to treat other significant human diseases.Read moreRead less