Novel Lysine-Rich Delivery Peptides of Plant Origin ERD and Human S100 The Effect of Carboxyfluorescein Conjugation, Influence of Aromatic and Proline Residues, Cellular Internalization, and Penetration Ability /
The need for novel drug delivery peptides is an important issue of the modern pharmaceutical research. Here, we test K-rich peptides from plant dehydrin ERD14 (ERD-A, ERD-B, and ERD-C) and the C-terminal CPP-resembling region of S100A4 (S100) using the 5(6)-carboxyfluorescein (Cf) tag at the N-termi...
Elmentve itt :
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| Dokumentumtípus: | Cikk |
| Megjelent: |
2021
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| Sorozat: | ACS OMEGA
6 No. 50 |
| Tárgyszavak: | |
| doi: | 10.1021/acsomega.1c04637 |
| mtmt: | 32491001 |
| Online Access: | http://publicatio.bibl.u-szeged.hu/24286 |
| Tartalmi kivonat: | The need for novel drug delivery peptides is an important issue of the modern pharmaceutical research. Here, we test K-rich peptides from plant dehydrin ERD14 (ERD-A, ERD-B, and ERD-C) and the C-terminal CPP-resembling region of S100A4 (S100) using the 5(6)-carboxyfluorescein (Cf) tag at the N-terminus. Via a combined pH-dependent NMR and fluorescence study, we analyze the effect of the Cf conjugation/modification on the structural behavior, separately investigating the (5)-Cf and (6)-Cf forms. Flow cytometry results show that all peptides internalize; however, there is a slight difference between the cellular internalization of (5)- and (6)-Cf-peptides. We indicate the possible importance of residues with an aromatic sidechain and proline. We prove that ERD-A localizes mostly in the cytosol, ERD-B and S100 have partial colocalization with lysosomal staining, and ERD-C mainly localizes within vesicle-like compartments, while the uptake mechanism mainly occurs through energy-dependent paths. |
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| Terjedelem/Fizikai jellemzők: | 34470-34484 |
| ISSN: | 2470-1343 |