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Design and synthesis of a novel peptide for selective detection of cancer cells
Author(s) -
Rajavenkatesh Krishnamoorthy,
Padmaja Murali,
Janani Indrakumar,
Aishwarya Satish,
Purna Sai Korrapati,
Thennarasu Sathiah
Publication year - 2020
Publication title -
chemical biology and drug design
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.59
H-Index - 77
eISSN - 1747-0285
pISSN - 1747-0277
DOI - 10.1111/cbdd.13675
Subject(s) - peptide , cancer cell , chemistry , popc , biophysics , biochemistry , lipid bilayer , cancer , membrane , biology , genetics
Using a minimalist approach, an 11‐residue peptide (Peptide 1 ) tagged with rhodamine fluorophore was designed and synthesized for selective detection of cancer cells. Peptide 1 contains RGD and NGR motifs to bind, respectively, integrins and aminopeptidase CD13, which are over expressed in cancer cells. Surface tension measurements revealed that peptide 1 possess surface‐active property owing to the overall hydrophobicity and cationic nature of the peptide. Peptide 1 displays cancer cell‐selective binding at ≤5.0 µM concentrations, while peptide 2 (randomized sequence of 1 ) shows non‐selective binding to normal and cancer cells. Fluorescence microscopy and FACS analysis demonstrated the intracellular localization of peptide 1 in three different cancer cell lines, confirming the role of RGD and NGR motifs. Cytotoxicity assay exhibited the viability of normal and cancer cells up to 100 µM concentrations of peptide 1 . Steady‐state fluorescence measurements disclosed the preferential interactions of the peptide 1 with anionic POPC/POPG bilayers rather than with zwitterionic POPC lipid bilayers. Circular dichroism studies showed minimal changes in the secondary structure of peptide 1 upon binding with the anionic lipid bilayers. Peptide 1 is largely unordered, non‐toxic, and useful for identification of cancer cells. Peptide 1 provides a template for designing drug‐loaded peptides for targeted delivery into cancer cells.