The impact of alpha-hydrazino acids embedded in short fluorescent peptides on peptide interactions with DNA and RNA (CROSBI ID 228161)
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Suć, Josipa ; Tumir, Lidija-Marija ; Glavaš-Obrovac, Ljubica ; Jukić, Marijana ; Piantanida, Ivo ; Jerić, Ivanka
engleski
The impact of alpha-hydrazino acids embedded in short fluorescent peptides on peptide interactions with DNA and RNA
Series of novel hydrazino-based peptidomimetics and analogues comprising N-terminal lysine and C-terminal phenanthridinyl-L-alanine were prepared. Presented results demonstrate up till now unknown possibility to finely modulate peptide interaction with DNA/RNA by α-hydrazino group insertion and how different positioning of two α-hydrazino groups in peptide controls binding to various double stranded and single stranded DNA and RNA. All peptidomimetics bind with 1-10 micromolar affinity to ds-DNA/RNA, whereby binding mode is combination of electrostatic interactions and hydrophobic interactions within DNA/RNA grooves. Insertion of α-hydrazino group into peptide systematically decreased its fluorimetric response to DNA/RNA binding in line: mono-hydrazino<alternating-hydrazino<sequential-hydrazino group. Binding studies to ss-polynucleotides suggest intercalation of phenanthridine between polynucleotide bases, whereby affinity and fluorimetric response decrease with the number of α-hydrazino groups in peptide sequence. Particularly interesting was interaction of two sequential α-hydrazino acids-peptidomimetic with poly rG, characterised by specific strong increase of CD bands, while all other peptide/ssRNA combinations gave only CD-bands decrease. All mentioned interactions could also be reversibly controlled by pH, due to the protonation of the fluorophore.
hydrazino ; peptidomimetic ; DNA/RNA ; interactions
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nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
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