Characterization of Rhodamine Conjugated Agiotensin II Peptide: Synthesis, Analysis and Receptor Binding and Internalization.

Title: Characterization of Rhodamine Conjugated Agiotensin II Peptide: Synthesis, Analysis and Receptor Binding and Internalization.

Volume: 9 Issue: 6

Author(s): Satya P. Yadav, Sadashiv Karnick, Wei-Zhen Shen and Jingli Zhang

Affiliation:

Keywords: peptides, angiotensin, receptor, lysine, valine, sarcosine, rhodamine, mass spectrometry

Abstract: The results in this study show that the rhodamine fluorophore can be specifically conjugated to Angiotensin II at Lys3 residue (substituted for a Val) without altering the biological activity of the parent compound. The conjugated peptide was characterized using HPLC, mass spectrometry, and N-terminal sequencing. The rhodamine-Angiotensin II binds effectively to AT1 receptor and gets internalized in clathrin coated vesicles by endocytosis. These results clearly suggest the usefulness of fluorophoreconjugated peptides in studies such as, ligand-receptor binding, and ligand-receptor complex internalization, for drug delivery using cell receptors and as an alternative to peptide hormone radioimmunoassays.

Cite this article as:

Yadav P. Satya, Karnick Sadashiv, Shen Wei-Zhen and Zhang Jingli, Characterization of Rhodamine Conjugated Agiotensin II Peptide: Synthesis, Analysis and Receptor Binding and Internalization., Protein & Peptide Letters 2002; 9 (6) . https://dx.doi.org/10.2174/0929866023408427