Naslov
Design of linear and cyclic peptides for ester hydrolysis

Autori
Sepčić, Sabino ; Janković, Patrizia ; Kalafatovic, Daniela

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

Skup
27 th Croatian Meeting of Chemists and Chemical Engineers (HSKIKI)

Mjesto i datum
Veli Lošinj, Hrvatska, 05.10.2021. - 08.10.2021

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
self-assembly, catalytic, peptides, minimalistic, cyclic

Sažetak
In chemistry, catalysts are substances that increase the rate of a reaction without being consumed itself. In nature, large protein assemblies which fold into specific three- dimensional structures with catalytic functions. Short peptides consisting of up to 10 amino acids can be exploited as catalysts for ester hydrolysis examined by the model reaction of para nitrophenyl acetate hydrolysis. For the purpose of testing the catalytic activity, we have chosen two peptides, IHIHINI and IHINIHI inspired by Rufo et al. These sequences should be able to self-assemble into catalytic amyloids that could act as Zn2+ - dependent esterases. We want to investigate the effect of changing the position of asparagine (N) on the self-assembly and catalytic properties of the proposed peptides. Peptides have been characterized by the LC-MS. There are many approaches for peptide cyclization. Our peptides will be designed through the addition of cysteine residues to allow the cyclization through a formation of a disulfide bridge between the thiol side chains of cysteine residues (Figure 4.). By using cyclization to form intra-connected peptide structures, we expect that the increased rigidity introduced by cyclization will improve the catalytic efficiency of short peptides.

Izvorni jezik
Engleski

Znanstvena područja
Interdisciplinarne prirodne znanosti, Biotehnologija, Interdisciplinarne biotehničke znanosti, Biotehnologija u biomedicini (prirodno područje, biomedicina i zdravstvo, biotehničko područje)

POVEZANOST RADA