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Dipeptides as potential anti-flammatory drugs for rheumatoid arthritis

Includes abstract.

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Bibliographic Details
Main Author: Mohajane, Mamohale
Other Authors: Jackson, Graham Ellis
Format: Thesis
Language:English
Published: Department of Chemistry 2014
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access_status_str Open Access
author Mohajane, Mamohale
author2 Jackson, Graham Ellis
author_browse Jackson, Graham Ellis
Mohajane, Mamohale
author_facet Jackson, Graham Ellis
Mohajane, Mamohale
author_sort Mohajane, Mamohale
collection Thesis
description Includes abstract.
format Thesis
id oai:open.uct.ac.za:11427/6340
institution University of Cape Town (South Africa)
language eng
last_indexed 2026-06-10T12:31:35.974Z
license_str Not specified — see source repository
provenance_str_mv Harvested via OAI-PMH from UCTD — University of Cape Town Open Access Repository
publishDate 2014
publishDateRange 2014
publishDateSort 2014
publisher Department of Chemistry
publisherStr Department of Chemistry
record_format dspace
source_str UCTD — University of Cape Town Open Access Repository
spelling oai:open.uct.ac.za:11427/6340 Dipeptides as potential anti-flammatory drugs for rheumatoid arthritis Mohajane, Mamohale Jackson, Graham Ellis Chemistry Includes abstract. Includes bibliographical references. The H⁺ and Cu²⁺ equilibria of four glycine peptides (glycyl-glycine, glycyl-L-leucine, glycyl-L-phenylalanine and glycyl-L-histidine) and four sarcosine peptides (sarcosylglycine, sarcosyl-L-leucine, sarcosyl-L-phenylalanine and sarcosyl-L-histidine) have been studied using glass electrode potentiometry and isothermal titration calorimetry at 25 °C and an ionic strength 0.15 M (NaCl). The terminal amine of the sarcosine peptides is more basic than the glycine analogues. The methyl group on the terminal amine (for sarcosine peptides) does not affect the stability constants of the ML species, significantly. Log K for ML species for all the Cu(II)/peptides complexes ranged between 5.79 and 6.54, except for glycyl-L-histidine that showed log KML = 9.16. Heat accompanying the formation of ML for all the species ranged between -5.1 kcal mol⁻¹ and-6.6 kcal mol⁻¹, except for glycyl-L-histidine that showed ΔHML = -3.6 kcal.mol⁻¹. Structures for the different species in solution were postulated based on nuclear magnetic resonance and ultraviolet-visible spectrophotometry data. Molecular mechanics was used to investigate the possible structures. The minimum energy of the trans form of most the complexes was less than the cis form of the complexes. 2014-08-13T14:27:22Z 2014-08-13T14:27:22Z 2013 Master Thesis Masters MSc http://hdl.handle.net/11427/6340 eng application/pdf Department of Chemistry Faculty of Science University of Cape Town
spellingShingle Chemistry
Mohajane, Mamohale
Dipeptides as potential anti-flammatory drugs for rheumatoid arthritis
thesis_degree_str Master's
title Dipeptides as potential anti-flammatory drugs for rheumatoid arthritis
title_full Dipeptides as potential anti-flammatory drugs for rheumatoid arthritis
title_fullStr Dipeptides as potential anti-flammatory drugs for rheumatoid arthritis
title_full_unstemmed Dipeptides as potential anti-flammatory drugs for rheumatoid arthritis
title_short Dipeptides as potential anti-flammatory drugs for rheumatoid arthritis
title_sort dipeptides as potential anti flammatory drugs for rheumatoid arthritis
topic Chemistry
url http://hdl.handle.net/11427/6340
work_keys_str_mv AT mohajanemamohale dipeptidesaspotentialantiflammatorydrugsforrheumatoidarthritis