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You searched for subject:(HCA II). Showing records 1 – 2 of 2 total matches.

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Mississippi State University

1. Wilson, David L. Human carbonic anhydrase II: preparation, metal-substitution, activity, and inhibition.

Degree: PhD, Chemistry, 2015, Mississippi State University

This report details the activities and inhibition of metal-substituted human carbonic anhydrase II (M-HCA-II). The traditional activities (hydrolysis of CO2 and <I>para</I>-nitrophenol acetate) in addition to new activities (oxidation of 2-aminophenol, disproportionation of H2O2, and disproportionation of superoxide) were investigated. Values reported for the relative hydrolytic activities of M-HCA-IIs are reported here for the first time, ranging from 47.5 % (plus or minus 0.6) to 86 % (plus or minus 4) for the hydrolysis of CO2 and from 0.299 % (plus or minus 0.012) to 4.72 % (plus or minus 0.015) for the hydrolysis of <I>para</I>-nitrophenol acetate. With respect to new activities, only the oxidation of 2-aminophenol was observed. Turnover was observed for Fe-HCA-II (kcat/KM = 3.6 plus or minus 1.3 mM-1 s-1) and Cu-HCA-II (kcat/KM = 8 plus or minus 2 mM-1 s-1). Inhibition of Zn-, (di-substituted) Cu2-, and Cu/Zn-HCA-II hydrolysis of CO2 and <I>para</I>-nitrophenol acetate by sulfanilamide, coumarin, and <I>ortho</I>-coumaric acid were investigated. Sulfanilamide was shown to inhibit: Zn-HCA-II, Cu2-HCA-II, and Cu/Zn-HCA-II - (with CO2) KM = 8.9 plus or minus 1.1 microM, 11 plus or minus 2 microM, 8.8 plus or minus 1.4 microM and (with p-nitrophenyl acetate) KM = 8.4 plus or minus 1.0 microM, (none), 8.4 plus or minus 1.4 microM, respectively. No inhibition was observed for coumarin or <I>ortho</I>-coumaric acid or its derivatives for any CAs studied. Advisors/Committee Members: Joseph P. Emerson (chair), Edwin A. Lewis (committee member), Todd E. Mlsna (committee member), Nicholas C. Fitzkee (committee member), Debbie J. Beard (committee member).

Subjects/Keywords: human carbonic anhydrase II; HCA-II; metal-substitution; copper; cobalt; manganese; iron; nickel; sulfanilamide; coumarin; kinetics; 2-aminophenol; catalase; superoxide dismutase; peroxidase

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Wilson, D. L. (2015). Human carbonic anhydrase II: preparation, metal-substitution, activity, and inhibition. (Doctoral Dissertation). Mississippi State University. Retrieved from http://sun.library.msstate.edu/ETD-db/theses/available/etd-06222015-164959/ ;

Chicago Manual of Style (16th Edition):

Wilson, David L. “Human carbonic anhydrase II: preparation, metal-substitution, activity, and inhibition.” 2015. Doctoral Dissertation, Mississippi State University. Accessed April 16, 2021. http://sun.library.msstate.edu/ETD-db/theses/available/etd-06222015-164959/ ;.

MLA Handbook (7th Edition):

Wilson, David L. “Human carbonic anhydrase II: preparation, metal-substitution, activity, and inhibition.” 2015. Web. 16 Apr 2021.

Vancouver:

Wilson DL. Human carbonic anhydrase II: preparation, metal-substitution, activity, and inhibition. [Internet] [Doctoral dissertation]. Mississippi State University; 2015. [cited 2021 Apr 16]. Available from: http://sun.library.msstate.edu/ETD-db/theses/available/etd-06222015-164959/ ;.

Council of Science Editors:

Wilson DL. Human carbonic anhydrase II: preparation, metal-substitution, activity, and inhibition. [Doctoral Dissertation]. Mississippi State University; 2015. Available from: http://sun.library.msstate.edu/ETD-db/theses/available/etd-06222015-164959/ ;

2. Vallade, Maëlle. Reconnaissance de surfaces de protéines par les foldamères d'oligoamides aromatiques : Protein surface recognition using aromatic oligoamide foldamers.

Degree: Docteur es, Chimie organique, 2016, Bordeaux

Les protéines étant au coeur d’un grand nombre de processus biologiques, elles sont des cibles thérapeutiques largement convoitées. Les foldamères, notamment les oligoamides aromatiques, présentent une structure bien définie, prévisible, stable en solution et à l’état solide. Ajouté à cela, leur taille moyenne en fait de bons candidats pour la reconnaissance de surfaces de protéines, grâce à leurs chaînes latérales protéinogènes. Cette thèse présente les différentes étapes de leur conception, de la synthèse de la brique constitutive à l’obtention d’un foldamère fonctionnalisé grâce à la synthèse en phase supportée. La stratégie d’investigation des interactions entre un foldamère et une protéine est détaillée. L’originalité réside dans le fait que le foldamère est ancré directement à la protéine et le dichroïsme circulaire sert de méthode de screening. L’analyse structurale des hits permet de générer de nouveaux foldamères dans le but d’améliorer les interactions avec la protéine : c’est une stratégie itérative. Cette approche est appliquée premièrement à l’anhydrase carbonique humaine II, protéine modèle qui sert de preuve de principe pour cette approche ; puis à des protéines d’intérêt thérapeutique plus important : l’interleukine 4 et la cyclophiline A. Enfin, une étude concernant l’introduction de flexibilité au sein de foldamères de quinolines est présentée.

Since proteins are at the basis of many biological processes, they are widely studied as therapeutic targets. Aromatic oligoamide foldamers have a very well defined structure, predictable and stable both in solution and solid state. Because of their medium size, they appear as potent candidates for protein surface recognition thanks to their proteinogenic side chains. This manuscript presents the different steps of their design, from the scaffold’s synthesis to obtaining a functionalized foldamer, thanks to solid phase synthesis. The strategy to investigate protein/foldamer interactions will be detailed. Its originality lies in the fact that the foldamer is anchored to the protein. Circular dichroism has been used as a screening method to detect foldamer/protein interactions. Structural analysis of the hits will allow the design of new foldamers with the objective of enhancing foldamer/protein interactions: it is an iterative strategy. This approach has been applied firstly to human carbonic anhydrase II (HCA). This protein is used as a model system and proof of concept before moving to more therapeutically relevant proteins; interleukin 4 and cyclophilin A. Finally, a study on introducing flexibility in quinoline foldamers is presented.

Advisors/Committee Members: Huc, Ivan (thesis director).

Subjects/Keywords: Foldamère d’oligoamides aromatiques; Reconnaissance de surface de protéine; Quinoline; Anhydrase carbonique humaine II (HCA),; Interleukine 4 (IL-4); Cyclophiline A (CypA); Analyse structurale; Cinétique d’inversion d’hélicité; Aromatic oligoamide foldamers; Protein surface recognition; Quinoline; Human carbonic anhydrase II (HCA); Interleukin 4 (IL-4); Cyclophilin A (CypA); Structural analysis; Kinetic of handedness inversion

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Vallade, M. (2016). Reconnaissance de surfaces de protéines par les foldamères d'oligoamides aromatiques : Protein surface recognition using aromatic oligoamide foldamers. (Doctoral Dissertation). Bordeaux. Retrieved from http://www.theses.fr/2016BORD0145

Chicago Manual of Style (16th Edition):

Vallade, Maëlle. “Reconnaissance de surfaces de protéines par les foldamères d'oligoamides aromatiques : Protein surface recognition using aromatic oligoamide foldamers.” 2016. Doctoral Dissertation, Bordeaux. Accessed April 16, 2021. http://www.theses.fr/2016BORD0145.

MLA Handbook (7th Edition):

Vallade, Maëlle. “Reconnaissance de surfaces de protéines par les foldamères d'oligoamides aromatiques : Protein surface recognition using aromatic oligoamide foldamers.” 2016. Web. 16 Apr 2021.

Vancouver:

Vallade M. Reconnaissance de surfaces de protéines par les foldamères d'oligoamides aromatiques : Protein surface recognition using aromatic oligoamide foldamers. [Internet] [Doctoral dissertation]. Bordeaux; 2016. [cited 2021 Apr 16]. Available from: http://www.theses.fr/2016BORD0145.

Council of Science Editors:

Vallade M. Reconnaissance de surfaces de protéines par les foldamères d'oligoamides aromatiques : Protein surface recognition using aromatic oligoamide foldamers. [Doctoral Dissertation]. Bordeaux; 2016. Available from: http://www.theses.fr/2016BORD0145

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