Naslov
The role of the amino acid chirality as the potential promoter of different types of turns in ferrocene peptides

Autori
Kodrin, Ivan ; Čakić Semenčić, Mojca ; Barišić, Lidija

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Book of abstracts, Math/Chem/Comp 2016 / Vančik, Hrvoj ; Cioslowski, Jerzy - , 2016, 4-4

Skup
Math/Chem/Comp 2016, 28th MC2 Conference

Mjesto i datum
Dubrovnik, Hrvatska, 20.06.2016. - 26.06.2016

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
conformational analysis; DFT (Density Functional Theory); ferrocene peptides; hydrogen bonding; NMR

Sažetak
Ferrocene and its derivatives have attracted much attention in recent years due to their specific structural properties and applications in bioorganometallic and bioanalytical chemistry. Ferrocene peptides show potential to mimick secondary structures of proteins. The distance of 3.3 Å between two cyclopentadienyl rings promotes intramolecular hydrogen bonding between peptide chains. [1] Recently, a series of mono- and disubstituted ferrocene peptide derivatives have shown the self-assembly and gelation behaviour. [2] A series of monosubstituted ferrocene peptides bearing homo- and heterochiral Pro-Ala sequence were described. A change of the Pro amino acid chirality can affect the secondary structure. A homochiral derivatives of t-BuCO-Pro-Ala-NHFc favour β-turns, and a disruption of the secondary structure, observed in their heterochiral analogues in solution, is ascribed to formation of γ-turns according to the computational study. In comparison to ferrocene conjugates, their non-ferrocene analogues comprised of the same amino acid sequences showed β-turn as the most preferred structural motif. Thus, a ferrocene unit could act as a potential promoter of γ-turns in heterochiral derivatives. The X-ray determined crystal structures of heterochiral derivatives show preference for β-turns. The calculated interaction energies pointed out the significance of the intermolecular hydrogen bonds favourable enough to overcome rearrangement of a single molecule from the most stable conformer to the one adopted in the solid state. The current research confirms the potential of the investigated compounds for the fine tuning of their conformational properties by variation of the chirality of constituted amino acids.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

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