mso-fareast-language:IT;mso-no-proof:yes">Herein, we described the synthesis of
two L-phenylalanines α-derivatized with a terminal alkyne moiety whose
structures differed by phenyl ring halogen substitution (two o-Cl in 1
vs. one p-Br in 2 ) and an investigation of their effect on biological
macromolecules and living cells. We explored their interaction with quadruplex
DNA (G4 DNA), using tel26 and c-myc as models, and bovine serum albumin (BSA).
By CD spectroscopy we found that 1 induced tel26 secondary structure
changes leading also to a slight thermal stabilization of this hybrid antiparallel/parallel
G4 structure, while the c-myc parallel topology remained essentially unchanged
upon 1 binding. Other CD evidences showed the ability of 1 to bind
BSA and mso-ansi-language:IT">molecular docking studies demonstrated that it could be
housed into the hydrophobic cavity between sub-domains IIA, IIB, and IIIA of
the protein .
Furthermore, concentration-dependent spectroscopic studies suggested the
ability of 1 to aggregate forming non-covalent polymeric systems in
aqueous solution. Differently from 1 , the bromine-modified compound was
able to bind Cu (II) ion, with the formation of a CuL 2
complex, as found by UV spectroscopy. Preliminary cell tests excluded cytotoxic
effect of both compounds towards normal cells, whereas showed a slight antiproliferative
effects for 2 on PC3 cancerous cells at 24 h, and for 1 on both
T98G and MDA-MB-231 cancer cells at 48 h.
|▼ Protein-Protein-Interaction network–disease relationship, pathogenicity and therapeutic perspectives Relazione tra malattia e alterate interazioni proteina-proteina: patogenicità e prospettive terapeutiche|
|▼ Targeting Sam-Sam interactions mediated by EphA2 receptor: design and evaluation of peptide inhibitors Progettazione e validazione di peptidi inibitori delle interazioni Sam-Sam mediate dal recettore EphA2|