Self-Assembling Multifunctional Peptide Dimers for Gene Delivery Systems
Self-assembling multifunctional peptide was designed for gene delivery systems. The multifunctional peptide (MP) consists of cellular penetrating peptide moiety (R8), matrix metalloproteinase-2 (MMP-2) specific sequence (GPLGV), pH-responsive moiety (H5), and hydrophobic moiety (palmitic acid) (CR8G...
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| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2015-01-01
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| Series: | Advances in Materials Science and Engineering |
| Online Access: | http://dx.doi.org/10.1155/2015/852584 |
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| author | Kitae Ryu Gyeong Jin Lee Ji-yeong Choi Taewan Kim Tae-il Kim |
| author_facet | Kitae Ryu Gyeong Jin Lee Ji-yeong Choi Taewan Kim Tae-il Kim |
| author_sort | Kitae Ryu |
| collection | DOAJ |
| description | Self-assembling multifunctional peptide was designed for gene delivery systems. The multifunctional peptide (MP) consists of cellular penetrating peptide moiety (R8), matrix metalloproteinase-2 (MMP-2) specific sequence (GPLGV), pH-responsive moiety (H5), and hydrophobic moiety (palmitic acid) (CR8GPLGVH5-Pal). MP was oxidized to form multifunctional peptide dimer (MPD) by DMSO oxidation of thiols in terminal cysteine residues. MPD could condense pDNA successfully at a weight ratio of 5. MPD itself could self-assemble into submicron micelle particles via hydrophobic interaction, of which critical micelle concentration is about 0.01 mM. MPD showed concentration-dependent but low cytotoxicity in comparison with PEI25k. MPD polyplexes showed low transfection efficiency in HEK293 cells expressing low level of MMP-2 but high transfection efficiency in A549 and C2C12 cells expressing high level of MMP-2, meaning the enhanced transfection efficiency probably due to MMP-induced structural change of polyplexes. Bafilomycin A1-treated transfection results suggest that the transfection of MPD is mediated via endosomal escape by endosome buffering ability. These results show the potential of MPD for MMP-2 targeted gene delivery systems due to its multifunctionality. |
| format | Article |
| id | doaj-art-268b96e8e5704926b95c17e626a5f9f3 |
| institution | Kabale University |
| issn | 1687-8434 1687-8442 |
| language | English |
| publishDate | 2015-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Advances in Materials Science and Engineering |
| spelling | doaj-art-268b96e8e5704926b95c17e626a5f9f32025-02-03T01:32:01ZengWileyAdvances in Materials Science and Engineering1687-84341687-84422015-01-01201510.1155/2015/852584852584Self-Assembling Multifunctional Peptide Dimers for Gene Delivery SystemsKitae Ryu0Gyeong Jin Lee1Ji-yeong Choi2Taewan Kim3Tae-il Kim4Department of Biosystems & Biomaterials Science and Engineering, College of Agriculture and Life Sciences, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-921, Republic of KoreaDepartment of Biosystems & Biomaterials Science and Engineering, College of Agriculture and Life Sciences, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-921, Republic of KoreaDepartment of Biosystems & Biomaterials Science and Engineering, College of Agriculture and Life Sciences, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-921, Republic of KoreaDepartment of Biosystems & Biomaterials Science and Engineering, College of Agriculture and Life Sciences, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-921, Republic of KoreaDepartment of Biosystems & Biomaterials Science and Engineering, College of Agriculture and Life Sciences, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-921, Republic of KoreaSelf-assembling multifunctional peptide was designed for gene delivery systems. The multifunctional peptide (MP) consists of cellular penetrating peptide moiety (R8), matrix metalloproteinase-2 (MMP-2) specific sequence (GPLGV), pH-responsive moiety (H5), and hydrophobic moiety (palmitic acid) (CR8GPLGVH5-Pal). MP was oxidized to form multifunctional peptide dimer (MPD) by DMSO oxidation of thiols in terminal cysteine residues. MPD could condense pDNA successfully at a weight ratio of 5. MPD itself could self-assemble into submicron micelle particles via hydrophobic interaction, of which critical micelle concentration is about 0.01 mM. MPD showed concentration-dependent but low cytotoxicity in comparison with PEI25k. MPD polyplexes showed low transfection efficiency in HEK293 cells expressing low level of MMP-2 but high transfection efficiency in A549 and C2C12 cells expressing high level of MMP-2, meaning the enhanced transfection efficiency probably due to MMP-induced structural change of polyplexes. Bafilomycin A1-treated transfection results suggest that the transfection of MPD is mediated via endosomal escape by endosome buffering ability. These results show the potential of MPD for MMP-2 targeted gene delivery systems due to its multifunctionality.http://dx.doi.org/10.1155/2015/852584 |
| spellingShingle | Kitae Ryu Gyeong Jin Lee Ji-yeong Choi Taewan Kim Tae-il Kim Self-Assembling Multifunctional Peptide Dimers for Gene Delivery Systems Advances in Materials Science and Engineering |
| title | Self-Assembling Multifunctional Peptide Dimers for Gene Delivery Systems |
| title_full | Self-Assembling Multifunctional Peptide Dimers for Gene Delivery Systems |
| title_fullStr | Self-Assembling Multifunctional Peptide Dimers for Gene Delivery Systems |
| title_full_unstemmed | Self-Assembling Multifunctional Peptide Dimers for Gene Delivery Systems |
| title_short | Self-Assembling Multifunctional Peptide Dimers for Gene Delivery Systems |
| title_sort | self assembling multifunctional peptide dimers for gene delivery systems |
| url | http://dx.doi.org/10.1155/2015/852584 |
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