Design and Synthesis of Near-Infrared Peptide for in Vivo Molecular Imaging of HER2.

ABSTRACT: We report the development, characterization, and validation of a peptide specific for the extracellular domain of HER2. This probe chemistry was developed for molecular imaging by using a structural model to select an optimal combination of amino acids that maximize the likelihood for unique hydrophobic and hydrophilic interactions with HER2 domain 3. The sequence KSPNPRF was identified and conjugated with either FITC or Cy5.5 via a GGGSK linker using Fmoc-mediated solid-phase synthesis to demonstrate flexibility for this chemical structure to be labeled with different fluorophores. A scrambled sequence was developed for control by altering the conformationally rigid spacer and moving both hydrophobic and hydrophilic amino acids on the C-terminus. We validated peptide specificity for HER2

SUBMITTER: Joshi BP 

PROVIDER: S-EPMC5384256 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature