l-Carnosine-Derived Fmoc-Tripeptides Forming pH-Sensitive and Proteolytically Stable Supramolecular Hydrogels
A series of β-amino acid containing tripeptides has been designed and synthesized in order to develop oligopeptide-based, thermoreversible, pH-sensitive, and proteolytically stable hydrogels. The Fmoc [N-(fluorenyl-9-methoxycarbonyl)]-protected tripeptides were found to produce hydrogels in both pH...
| Publié dans: | Langmuir : the ACS journal of surfaces and colloids. - 1985. - 33(2017), 45 vom: 14. Nov., Seite 12989-12999 |
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| Auteur principal: | |
| Autres auteurs: | , |
| Format: | Article en ligne |
| Langue: | English |
| Publié: |
2017
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| Accès à la collection: | Langmuir : the ACS journal of surfaces and colloids |
| Sujets: | Journal Article Research Support, Non-U.S. Gov't |
| Résumé: | A series of β-amino acid containing tripeptides has been designed and synthesized in order to develop oligopeptide-based, thermoreversible, pH-sensitive, and proteolytically stable hydrogels. The Fmoc [N-(fluorenyl-9-methoxycarbonyl)]-protected tripeptides were found to produce hydrogels in both pH 7 and 2 buffers at a very low concentration (<0.2% w/v). It has been shown that the Fmoc group plays an important role in the gelation process. Also a dependence of gelation ability on hydrophobicity of the side chain of the Fmoc-protected α-amino acid was observed. The effect of the addition of inorganic salts on the gelation process was investigated as well. Spectroscopic studies indicated formation of J-aggregates through π-π stacking interactions between Fmoc groups in solution as well as in the gel state. In the gel phase, these self-assembling tripeptides form long interconnected nanofibrils leading to the formation of 3-dimensional network structure. The hydrogels were characterized by various techniques, including field emission electron microscopy, transmission electron microscopy, atomic force microscopy, rheology, Fourier transform IR, circular dichroism (CD), and wide-angle X-ray diffraction (WAXD) spectroscopy. The CD studies and WAXD analyses show an antiparallel β-sheet structure in the gel state. l-Phenylalanine and l-tyrosine containing tripeptides formed helical aggregates with handedness opposite to those containing l-valine and l-leucine residues. The mechanical stability of the hydrogels was found to depend on the hydrophobicity of the side chain of the tripeptide as well as on the pH of the solution. Also, the tripeptides exhibit in vitro proteolytic stability against proteinase K enzyme |
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| Description: | Date Completed 31.07.2018 Date Revised 31.07.2018 published: Print-Electronic Citation Status PubMed-not-MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/acs.langmuir.7b03018 |