Metal binding and catalytic activity of macrocyclic peptides.
Aldous, Amanda.
2016
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Abstract: Metalloenzymes have specialized roles in biology which have been
refined by nature over time. The efficient and selective catalytic activity of
metalloenzymes is a characteristic that has been studied for decades and continues to be
desired of mimetic complexes. For synthetic catalysts, balancing needs for appropriate
recognition motifs, transition state stabilization of the reaction, ... read moreand robust activity has
been challenging. Well-designed metallopeptides help to meet this challenge by mimicking
native metalloenzymes in structure and composition, but also by emulating similar activity
as synthetic catalysts. Decades of studies have investigated the interactions of transition
metal ions with linear peptides; however conformationally constrained peptides have not
been as rigorously explored. The work discussed herein represents an effort to improve the
metal-binding and catalytic activity of a peptide-metal complex by incorporating a
macrocyclic constraint. This work is unique in its approach in that it uses
macrocyclization to tune chiral and functional catalytic sites of short peptide sequences.
This dissertation also explores the incorporation of metal-binding functionality into
peptide scaffolds in a new, synthetically accessible manner. This strategy represents a
potentially broad paradigm for generating asymmetric catalysts. This work has established
the fundamentals of the strategy, enabling the discovery of novel classes of constrained
metallopeptide scaffolds with observable catalytic reactivity.
Thesis (Ph.D.)--Tufts University, 2016.
Submitted to the Dept. of Chemistry.
Advisor: Joshua Kritzer.
Committee: Krishna Kumar, Elena Rybak-Akimova, and Elizabeth Nolan.
Keywords: Chemistry, Biochemistry, and Inorganic chemistry.read less - ID:
- 8910k5530
- Component ID:
- tufts:21172
- To Cite:
- TARC Citation Guide EndNote
