Date of Award
1-1-2017
Language
English
Document Type
Master's Thesis
Degree Name
Master of Science (MS)
College/School/Department
Department of Chemistry
Content Description
1 online resource (ii, vi, 137 pages) : illustrations (some color)
Dissertation/Thesis Chair
QIANG ZHANG
Keywords
Peptides, Thiols
Subject Categories
Chemistry
Abstract
The association between sterically requesting peptidyl destinations is hard to accomplish. The ligation between amino acids, for example, Val-Val has been ended up being amazingly testing with ordinary NCL strategies that are depending on exogenous thiol added substances. Besides, the extra of overabundance measures of outer thiol activators, for example, a 4-mercaptophenylacetic corrosive (MPAA) impede the consequent desulfurization, and it needs the additional progression to be expelled. Although various methodology has been produced to encourage MPAA expulsion, reverse phase preparative HPLC purification remains the best. Nevertheless, the additional purification decreases response proficiency and yield. Thus, we report a β-thiolactone-mediated additive-free native chemical ligation protocol that empowers the associations between the sterically requesting amino acid sites, and the fast NCL was trailed by the in situ dethionylation. Reaction rates between β-thiolactones and the customary thioester toward NCL were likewise examined to discount the direct aminolysis pathway. At last, we have prevailing with regards to orchestrating a gathering of dipeptides, tripeptides, and tetrapeptides. The reaction rate of β-thiolactones was way quicker than the customary thioester toward NCL. We concluded that the β-thiolactone-mediated additive-free native chemical ligation protocol had been turned out to be a superior strategy to accomplish the association between sterically requesting peptidyl sites than the regular NCL strategies. At long last, the potent cytotoxic cyclic-peptide axinastatin 1 has been readied utilizing the developed methodology.
Recommended Citation
Xiao, Yunxian, "Coupling of sterically demanding peptides by strain driven beta-thiolactone mediated native chemical ligation" (2017). Legacy Theses & Dissertations (2009 - 2024). 1980.
https://scholarsarchive.library.albany.edu/legacy-etd/1980