Reversible photo-control of peptide helix content:  Adjusting thermal stability of the cis state.
Contributors: University of Toronto.  Dept. of Chemistry.
Published: 2004
Language: eng
Number of pages: 116
Description: Photochemical switches can be used to control the secondary structure of peptides and proteins. For this purpose, we created and studied a series of azobenzene cross-linkers analogous to the Kumita compound (Kumita  et al., 2000), a symmetrical reagent 4,4' -bis(iodoacetamide)azobenzene, but with a range of thermal stabilities. To increase the rate of thermal reversion, derivatives with enhanced delocalization of the lone pair electrons of the para amino were designed. High reactivity and selectivity toward Cys residues was achieved by introducing methanethiosulfonyl groups. These groups enable reversible attachment of the cross-linker to peptides and proteins via disulfide linkages. The effects of the cross-linkers on the conformation of a test peptide (FK*-11) were evaluated. Second, a series of "long" azobenzene cross-linkers, containing two Cys-reactive chloroacetamide- and iodoacetamide-diphenylethynyl moieties that are linked to the azobenzene chromophore was designed and synthesized.
Notes: Adviser:  Andrew Woolley.

Thesis (M.Sc.)--University of Toronto, 2004.

Electronic version licensed for access by U. of T. users.

Source: Masters Abstracts International, Volume: 43-03, page: 0849.

MICR copy on microfiche (2 microfiches).