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

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

Journal Name: Protein & Peptide Letters

Volume 9 , Issue 6 , 2002

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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.

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

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Article Details

VOLUME: 9
ISSUE: 6
Year: 2002
Page: [465 - 476]
Pages: 12
DOI: 10.2174/0929866023408427
Price: $58

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