Post-graduate theses
Current Record: 563 of 642
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| Identifier |
uch.chemistry.msc//2002MST1102 |
| Title |
Σύνθεση "υποβιβλιοθήκης" φθοριζόντων τετραπεπτιδίων για τον προσδιορισμό εξειδίκευσης υποστρώματος της θέσης P2 πρωτάσεων σερίνης |
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Author
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Ρογκάκος, Βασίλειος
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| Abstract |
In the first chapter, the features and the principles of the enzymes action are presented. We define the proteolytic enzymes and their families. Particularly we define the serine proteases, the general catalytic mechanism and their substrate specificity. The human kallikreins are a subfamily of serine proteases. Protease M is a recently discovered member of this subfamily. Structural information and other important data about protease M are reported. In the second chapter the general principles of the fluorescence are analyzed. The general type of the fluorescent substrates for proteases is presented and some examples of compounds used as fluorescent markers and others as quenchers are given. In the third chapter, the solid phase peptide synthesis is described. The basic principles of the Fmoc/But strategy and the common coupling methods are described. Some examples of safety-catch linkers are given. In the fourth chapter the principles of Combinatorial Chemistry are presented. The synthetic routes to peptide libraries are described. Peptide libraries are categorized and their biological application is briefly discussed. The deconvolution of mixture based combinatorial libraries is explained. The detailed synthesis of sublibrary of fluorogenic tetrapepides for determining P2 substrate specificity of protease M and other enzymes is developed in the fifth chapter. The sublibrary P2 consists of 19 sub-sublibraries of the general type Αc-[X]-[X]-[O]-Lys-AMC, where [X] represents mixtures of 19 amino acids and [O] a spatially addressed amino acid for each sub-sublibrary. We conducted a limited chemical characterization of two sub-sublibraries by means of Electrospray mass spectrometry. Finally the enzymatic results for protease M, human kallikrein 15 and trypsin are given. In the experimental part, the synthetic routes in solid phase and solution, the identification of the products and the enzymatic assay are presented.
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| Language |
Greek |
| Issue date |
2002-07-01 |
| Collection
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School/Department--School of Sciences and Engineering--Department of Chemistry--Post-graduate theses
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Type of Work--Post-graduate theses
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| Permanent Link |
https://elocus.lib.uoc.gr//dlib/8/c/d/metadata-dlib-2002MST1102.tkl
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| Views |
180 |
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