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Fibrous Aggregates of Short Peptides Containing Two Distinct Aromatic Amino Acid Residues.

Wojciech LipinskiJoanna WaskoMalgorzata WalczakJustyna FraczykZbigniew J KaminskiKrystian GaleckiZbigniew DraczynskiIzabella KrucinskaMarta KaminskaBeata Kolesinska
Published in: Chemistry & biodiversity (2019)
The aim of the study was the assessment of the ability of short peptides to form aggregates under physiological conditions. The dipeptides studied were derived from different aromatic amino acids (heteroaromatic peptides). Tripeptides were obtained from two distinct aromatic amino acids and cysteine or methionine residue in the C-terminal, N-terminal, or central position. The ability of the peptides to form fibrous aggregates under physiological conditions was evaluated using three independent methods: the Congo Red assay, the Thioflavin T assay, and microscopic examinations using normal and polarized light. Materials potentially useful for regenerative medicine were selected based on their cytotoxicity to the endothelial cell line EA.hy 926 and physicochemical properties of films formed by peptides. The required parameters of biocompatibility were fulfilled by H-PheCysTrp-OH, H-PheCysTyr-OH, H-PheTyrMet-OH, and H-TrpTyr-OH.
Keyphrases
  • amino acid
  • high throughput
  • endothelial cells