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...
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| Main Authors: | |
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| Format: | Article |
| Published: |
2021
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| Series: | ACS OMEGA
6 No. 50 |
| Subjects: | |
| doi: | 10.1021/acsomega.1c04637 |
| mtmt: | 32491001 |
| Online Access: | http://publicatio.bibl.u-szeged.hu/24286 |
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| 024 | 7 | |a 10.1021/acsomega.1c04637 |2 doi | |
| 024 | 7 | |a 32491001 |2 mtmt | |
| 040 | |a SZTE Publicatio Repozitórium |b hun | ||
| 041 | |a Angol | ||
| 100 | 1 | |a Sebák Fanni | |
| 245 | 1 | 0 | |a Novel Lysine-Rich Delivery Peptides of Plant Origin ERD and Human S100 |h [elektronikus dokumentum] : |b The Effect of Carboxyfluorescein Conjugation, Influence of Aromatic and Proline Residues, Cellular Internalization, and Penetration Ability / |c Sebák Fanni |
| 260 | |c 2021 | ||
| 300 | |a 34470-34484 | ||
| 490 | 0 | |a ACS OMEGA |v 6 No. 50 | |
| 520 | 3 | |a 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. | |
| 650 | 4 | |a Kémiai tudományok | |
| 650 | 4 | |a Általános orvostudomány | |
| 700 | 0 | 1 | |a Horváth Lilla Borbála |e aut |
| 700 | 0 | 1 | |a Kovács Dániel |e aut |
| 700 | 0 | 1 | |a Szolomájer János |e aut |
| 700 | 0 | 1 | |a Tóth Gábor |e aut |
| 700 | 0 | 1 | |a Babiczky Ákos |e aut |
| 700 | 0 | 1 | |a Bősze Szilvia |e aut |
| 700 | 0 | 1 | |a Bodor Andrea |e aut |
| 856 | 4 | 0 | |u http://publicatio.bibl.u-szeged.hu/24286/1/acsomega.1c04637.pdf |z Dokumentum-elérés |