Development of new supramolecular nanostructured materials based on peptide hydrogelator Ac-L-Phe-L-Phe-L-Ala-NH2 with embedded liposomes for potential biomedical application (CROSBI ID 667939)
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Podaci o odgovornosti
Frkanec, Ruža ; Radović, Karmen ; Štimac, Adela ; Horvat, Lucija ; Frkanec, Leo
engleski
Development of new supramolecular nanostructured materials based on peptide hydrogelator Ac-L-Phe-L-Phe-L-Ala-NH2 with embedded liposomes for potential biomedical application
In recent years design and synthesis of self- assembled nanomaterials with diversified structures and functionalities via fine tuning of supramolecular building blocks increased rapidly.1 Self-assembling peptides have been widely recognized as nanomaterials with high potential for a extensive range of biomedical applications from drug delivery to tissue enginering, owing to their hydrophilic character and biocompatibility.2, 3 The aim of the present study was preparation and characterization of supramolecular systems based on peptide hydrogelator4 Ac-L-Phe-L- Phe-L-Ala-NH2 and liposomes with incorporated model proteins. The gelling properties of the hydrogelator Ac-L-Phe-L-Phe-L-Ala-NH2 with addition of liposomes and proteins were studied. Liposome formulations of BSA and FITC-BSA incorporated in the hydrogel were characterized by electron and confocal microscopy. Transmission electron microscopy (TEM) confirmed incorporation of liposomes into the hydrogel. In gel samples with built-in BSA, the gel network preserved integrity, but it was noticed that the gel fibers were thinner and thicker. Confocal microscopy proved the incorporation of liposome formulations of FITC- BSA in the hydrogel. It was also shown that liposomes do not impair the gel network of hydrogelator at lipid concentrations lower than the gelator concentration. We confirmed that use of higher amounts of protein albumin (BSA)/FITC-BSA resulted in slower gel formation or inability to transition into gel. In order to investigate the potential of using the prepared nanostructured supramolecular systems in immunodiagnostic and immunotherapy, complex protein mixture isolated from allergen pollen of Ambrosia elatior plant was successfully incorporated into the tested system. 1. J. Boekhoven , W. E. Hendriksen , G. J. M. Koper , R. Eelkema , J. H. van Esch , Science 2015 , 349 , 1075 2. X. Du, J. Zhou, J. Shi, B. Xu, Chem. Rev. 2015, 115, 13165−13307, DOI: 10.1021/acs.chemrev.5b00299 3. R. Dong, Y. Pang, Y. Su, X. Zhu, Biomater. Sci., 2015, 3, 937. 4. T. Pospišil, L. Ferhatović Hamzić, L. Brkić Ahmed, M. Lovrić, S. Gajović, L. Frkanec, Biomater Sci. 2016 ; 4: 1412–1416.
supramolecular assembly ; peptide hydrogelators ; liposomes ; nanomaterials
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Podaci o prilogu
110-110.
2018.
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objavljeno
Podaci o matičnoj publikaciji
Journal of peptide science
Moroder, Luis
Chichester: John Wiley & Sons
1075-2617
1099-1387
Podaci o skupu
35th European Peptide Symposium
poster
26.08.2018-31.08.2018
Dublin, Irska
Povezanost rada
Biotehnologija u biomedicini (prirodno područje, biomedicina i zdravstvo, biotehničko područje), Kemija, Temeljne medicinske znanosti