Wyniki wyszukiwania - BazTech

Ograniczanie wyników

1 Wiadomości Chemiczne

1 2024

Znaleziono wyników: 1

Liczba wyników na stronie

Wyniki wyszukiwania

Wyszukiwano:
w słowach kluczowych: kallikreina 13

Sortuj według:

Ogranicz wyniki do:

Peptydy z węzłem cysteinowym jako inhibitory kallikreiny 13

Jankowska Dżesika, Rejmak Wiktoria, Lesner Adam, Gruba Natalia

Wiadomości Chemiczne

2024

[Z] 78, 3-4

346--368

Inhibitor cysteine knots (ICK) also known as "knottins," are cysteine-rich peptides typically composed of approximately 30 amino acids. These peptides exhibit a characteristic robust structure featuring three antiparallel β-sheets that are "knotted" together by three disulfide bonds. This structural motif confers stability to the protein, rendering it resistant to thermal denaturation and proteolysis. Consequently, inhibitor cysteine knots hold great promise as scaffolds for developing new peptide drugs. In this study, we present the synthesis and evaluation of six potential inhibitors targeting KLK13, utilizing the Ecballium elaterium trypsin II inhibitor (EETI-II) as the leading structure. The peptides were synthesized in solid-phase peptide synthesis with an automated peptide synthesizer. Subsequently, they were oxidized using iodine and then quenched with an anion exchange resin. Both linear and oxidized compounds were obtained and subjected to kinetic studies. The inhibitory activity against KLK13 was observed exclusively in the oxidized analogues of the synthesized compounds. Linear peptides exhibited lower affinity towards KLK13, highlighting the critical role of the disulfide bridge in the structure of the EETI-II analogues for inhibiting the enzyme activity.