Tailoring peptidomimetics for different functions (CROSBI ID 642049)
Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | međunarodna recenzija
Podaci o odgovornosti
Jerić ; Ivanka
engleski
Tailoring peptidomimetics for different functions
Design and synthesis of peptidomimetics represent an important field in chemistry, pharmacology and material science, as they circumvent the numerous limitations of natural peptides. Self-structural organizations important for biological functions of peptide and proteins, such as turns, helices, sheets and loops, can be accessed by chemical modifications of amino acids or peptides. These modifications include restriction of conformations performed either by the peptide cyclization or by the incorporation of conformationally constrained elements. In this presentation, two types of peptidomimetics will be presented: enediyne-based peptidomimetics and hydrazino peptidomimetics. Small molecule tweezers based on amino acids bridged with rigid cis-enediyne moiety showed high affinity for Cu(II), comparable with affinities of much larger peptides with incorporated typical Cu(II) binding sites, like Hys or Cys. [1] Next, bidentate triphenylphosphane amino acid ligands containing linkers with different flexibilities have been synthesized and their rhodium complexes were used as catalysts in asymmetric hydrogenation of α, β-unsubstituted amino acids. The nature of the linker in the bidentate ligands has a major influence on the selectivity in catalysis. In particular, enantioselectivities up to 81% ee were obtained with ligand containing enediyne-type of linker. [2] Finally, cyclic enediyne–amino acid chimeras were designed with the aim to inhibit aminopeptidase N (APN). Enediyne moiety was embedded within the 12-membered ring with hydrophobic amino acid Ala, Val, Leu or Phe used as carriers. APN inhibition test showed that enediyne-fused amino acids have potential as new pharmacophores in the design of APN inhibitors. [3] Replacement of Cβ atom in β-amino acids with nitrogen leads to hydrazino peptides, a class of peptidomimetics able to adopt various secondary structures. A series of hydrazino-based peptidomimetics were prepared for interaction with DNA/RNA. We showed that these interactions can be finely modulate by number and position of α-hydrazino groups, whereby the binding mode is a combination of electrostatic interactions and hydrophobic interactions within DNA/RNA grooves. [4]
peptidomimetics; DNA/RNA interactions; enzyme inhibitors; enediynes; α-hydrazino acids
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Podaci o prilogu
2016.
objavljeno
Podaci o matičnoj publikaciji
22. Slovenian chemical days
Kaučić, V., Bešter-Rogač, M., Gantar, M.
Ljubljana: Slovesnko kemijsko društvo
978-961-93849-2-3
Podaci o skupu
22. Slovenian chemical days
pozvano predavanje
28.09.2016-30.09.2016
Portorož, Slovenija