Abstract
Cell-penetrating peptide (CPP) is a promising cargo for delivering bioactive molecules. In this study, the N terminus of VP1 from chicken anemia virus, designated as CVP1, was found to carry enriched arginine residues with α-helix. By confocal imaging, flow cytometry and MTT assay, we identified CVP1 as a novel, safe and efficient CPP. CVP1-FITC peptide could entry different types of cells tested with dose dependence, but without cytotoxic effects. Compared with TAT-FITC peptide, the CVP1-FITC peptide showed much higher cell-penetrating activity. Moreover, CVP1 could successfully deliver β-glycosidase, poly (I:C) and plasmid into HCT116 cells. Inhibitors and temperature sensitivity analysis further indicated that the cell-penetrating activity of CVP1 was based on ATP-dependent and caveolae-mediated endocytosis. All these data demonstrate that CVP1 has efficient cell-penetrating activity and great potential for developing a novel delivery vector.
Highlights
Cell-penetrating peptide (CPP) is an active cargo for delivering bioactive molecules into cells [1]
CPPs from VP1 protein N-terminus (CVP1) carried enriched argnine residues with α‐helix By the sequence alignment, we found that the N-terminus of the VP1 of chicken anemia virus (CAV), designated as CVP1, was highly conserved, and rich in arginine residues (Figure 1A)
Since the cationic CPPs generally carry multiple basic amino acids, the CVP1 sequence was submitted to the CellPPD server to evaluate its potential cell-penetrating activity
Summary
Cell-penetrating peptide (CPP) is an active cargo for delivering bioactive molecules into cells [1]. CPPs are composed of 5–30 amino acids (aa) with enriched lysine or arginine residues, and divided into three classes including amphipathic CPP, cationic CPP and hydrophobic CPP [2, 3]. As the pioneer of CPPs, HIV-TAT with 86 amino acids plays vital roles in the replication of HIV. It was reported that HIV-TAT contains enriched arginine and lysine residues with α-helical structure which play a key role in cell penetrating capacity [4, 5]. TAT peptide sequence contains a motif that is recognized and cleaved by furin so that its stability and cell penetrating capacity would be removed during the process to deliver exogenous cargoes [8]. A more efficient novel cell penetrating peptide needs to be developed
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
