Naslov
Synthesis of enediyne-bridged peptide for cell lysis

Autori
Jerić, Ivanka ; Chen, Hueih-Min

Vrsta, podvrsta i kategorija rada
Poglavlja u knjigama, ostalo

Knjiga
Peptides 2004

Urednik/ci
Flegel, Martin et. al.

Izdavač
Kenes Group

Grad
Ženeva

Godina
2005

Raspon stranica
218-219

ISBN
965-90833-0-0

Ključne riječi
enediynes, peptides

Sažetak
Antibacterial peptides represent a class of small proteins originally found in insects, but now shown to be widely distributed in animals and humans. Their ability of lysing bacterial cells attracts worldwide interest, especially nowadays when we are faced with bacterial resistance toward even the latest generation of antibiotics. Furthermore, many antibacterial peptides show promising anticancer activity without damaging normal eukaryotic cells. The distribution of the net charge of the peptide is recognized to be in direct correlation with biological function. Previous studies have shown that additional cationic residues in synthetic analogs of the antibacterial peptide cecropin B, contribute to higher efficiency in cancer cell lysis, as compared to the natural peptide. Also, conformational studies have confirmed a more compact form for the synthetic than for the native peptides. The decreased flexibility of the bend angle may be one of the factors leading to the higher cancer cell lysis ability. Following this assumption, we focus our interest on the hinge region by preparing models with an enediyne unit bridging two peptide fragments. The presence of a conformationally more defined spacer is expected to influence the pre-organization of the two carrying helices and thereby membrane permeability efficiency.

Izvorni jezik
Engleski

POVEZANOST RADA