Journal
ARABIAN JOURNAL OF CHEMISTRY
Volume 13, Issue 1, Pages 1966-1974Publisher
ELSEVIER
DOI: 10.1016/j.arabjc.2018.02.014
Keywords
Peptidyl nucleoside; Self-assembly; Drug-protein binding; Serum protein
Categories
Funding
- Regione Campania
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This article describes the synthesis of Thy-(Phe-Phe) and Thy-(Tyr-Tyr), two thyminebearing dipeptides based on L-phenylalanine and L-tyrosine, the circular dichroism (CD), UV and dynamic light scattering (DLS) characterization of their self-assemblies, and a CD study of their interaction with nucleic acids (using homoadenine DNA and RNA) and serum proteins (utilizing BSA as a model protein). DLS studies, alongside with CD and UV investigations conducted on aqueous solutions of the derivatives under different concentration and temperature conditions, showed the formation of extensive molecular architectures with hydrodynamic mean diameters higher than 300 nm, with Thy-(Tyr-Tyr) forming at pH = 7.5 particularly large and stable networks, involving multiple units, connected by H-bonding, aromatic and hydrophobic interactions. Finally, the findings of our study suggested that Thy-(Phe-Phe) and Thy-(Tyr-Tyr), very stable in human serum, were able to bind BSA protein altering its secondary structure. (C) 2018 Production and hosting by Elsevier B.V. on behalf of King Saud University.
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