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Search for Fibrous Aggregates Potentially Useful in Regenerative Medicine Formed under Physiological Conditions by Self-Assembling Short Peptides Containing Two Identical Aromatic Amino Acid Residues.
- Source :
-
Molecules (Basel, Switzerland) [Molecules] 2018 Mar 02; Vol. 23 (3). Date of Electronic Publication: 2018 Mar 02. - Publication Year :
- 2018
-
Abstract
- This study investigates the propensity of short peptides to self-organize and the influence of aggregates on cell cultures. The dipeptides were derived from both enantiomers of identical aromatic amino acids and tripeptides were prepared from two identical aromatic amino acids with one cysteine or methionine residue in the C-terminal, N-terminal, or central position. The formation or absence of fibrous structures under physiological conditions was established using Congo Red and Thioflavine T assays as well as by microscopic examination using normal and polarized light. The in vitro stability of the aggregates in buffered saline solution was assessed over 30 days. Materials with potential for use in regenerative medicine were selected based on the cytotoxicity of the peptides to the endothelial cell line EA.hy 926 and the wettability of the surfaces of the films, as well as using scanning electron microscopy. The criteria were fulfilled by H- d Phe d Phe-OH, H- d Cys d Phe d Phe-OH, H-CysTyrTyr-OH, H- d Phe d Phe d Cys-OH, H-TyrTyrMet-OH, and H-TyrMetTyr-OH. Our preliminary results suggest that the morphology and cell viability of L919 fibroblast cells do not depend on the stereochemistry of the self-organizing peptides.
- Subjects :
- Animals
Benzothiazoles
Cell Line
Cell Line, Tumor
Cell Survival drug effects
Congo Red
Dipeptides pharmacology
Fibroblasts cytology
Fibroblasts drug effects
Mice
Oligopeptides pharmacology
Protein Aggregates
Regenerative Medicine
Thiazoles
Tissue Engineering
Amino Acids chemistry
Dipeptides chemistry
Oligopeptides chemistry
Tissue Scaffolds
Subjects
Details
- Language :
- English
- ISSN :
- 1420-3049
- Volume :
- 23
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Molecules (Basel, Switzerland)
- Publication Type :
- Academic Journal
- Accession number :
- 29498711
- Full Text :
- https://doi.org/10.3390/molecules23030568