The design and synthesis of a light activatable beta-turn scaffold and its incorporation into cyclic peptides and dimerization inhibitors of HIV-1 protease

Luckner Gerard Ulysse, Purdue University

Abstract

A light activatable $\beta$-turn scaffold was designed and incorporated into cyclic peptides. The scaffold is an azobenzene molecule capable of adopting two distinct isomeric trans and cis forms. The scaffold was designed to template the $\beta$-turn conformation in small cyclic peptides upon irradiation with light. The peptide was designed such that, when the azobenzene was in the trans form the attached peptide adopted an extended conformation, whereas upon activation with light to the cis form, a $\beta$-turn was templated. This new scaffold templated a type II $\beta$-turn in one cyclic peptide and a type II$\sp\prime$ $\beta$-turn in a Somatostatin analog.

Degree

Ph.D.

Advisors

Chmielewski, Purdue University.

Subject Area

Organic chemistry|Biochemistry

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