Event Information
Functional Oligomers from Aryl 1,2,3 Triazoles
- Abstract:
Nature relies on biopolymers such as proteins to perform sophisticated tasks such as molecular recognition and catalysis efficiently. Mastery over noncovalent forces such as hydrogen bonding enables proteins to adopt stable, compact solution conformations which are fundamentally responsible for their complexity in structure and function. Considering these macromolecules are composed of only 20 unique monomer amino acids, the range of chemical capabilities displayed by proteins is quite remarkable. Designing analogous capabilities into unnatural polymer backbones that fold into well defined secondary structures (foldamers) is an emerging field inspired by biology.
This work reports a new type of foldamer scaffold, based on 1,4-diaryl-1,2,3-triazoles, that adopts helical conformations stabilized by C-H•••anion hydrogen bonding like interactions with anions. Previously considered insignificant, C-H•••X- interactions show promise as a novel interaction by which to manipulate and control secondary structure and function in rationally designed folding oligomers. The design, synthesis, and conformational analysis of 1,4-diaryl-1,2,3-triazole oligomers and their anion recognition function will be discussed.
Ph.D. Defense Examination Seminar
Student Exams Seminar