Naslov
Structural asymmetries and biological activity of membrane-transforming-peptides

Autori
Juretić, Davor

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

Izvornik
Book of Abstracts: Visualization and modeling in Chemistry / - Split, 2010

Skup
Visualization and modeling in Chemistry

Mjesto i datum
Split, Hrvatska, 29.10.2010. - 31.10.2010

Vrsta sudjelovanja
Pozvano predavanje

Vrsta recenzije
Nije recenziran

Ključne riječi
membranes; antimicrobial peptides; cell-penetrating peptides; amphipathic; structural asymmetries

Sažetak
Membranes have multifunctional and vital roles in all living cells. Less recognized fact is that membranes are mainly composed of amphipathic lipids with asymmetric distribution between outer and inner membrane leaflets, which is significantly different for cytoplasmic membrane of Gram-positive bacteria, Gram-negative bacteria, mammalian and cancer cells. Fusogenic peptides, cell-penetrating peptides and antimicrobial peptides are all the subject of intensive research during last 25 years as membrane-active peptides, due to potential applications in medicine, health care, food production and preservation, but published results describing how their structure and mechanism of action are connected with biological activity are often speculative and even contradictory. Taking amphipathic helical peptides as a common example, different types of helical peptides are usually classified according to biological activity, which can differ for several orders of magnitudes, even when their mean physicochemical properties are similar. It is likely that helical peptides may exhibit very different mechanisms of perturbing and restructuring biological membranes, depending on membrane type, peptide sequence and ionic strength of a solution. For the example of anuran antimicrobial peptides acting on Gram-negative bacteria and human red blood cells, we shall see that structural asymmetries in peptide primary structure can distinguish those with hemolytic properties, those with selective activity as mediocre peptide antibiotics and those with selective activity as excellent peptide antibiotics. Visualization tools should be able to see similar asymmetries in peptide 3D structure, but peptide backbone structure is certainly not enough for the job. We shall explore in this work how structural asymmetries due to residue type, sequence position and orientation in peptide helical structure may be connected to membrane-transforming and biological activity.

Izvorni jezik
Engleski

Znanstvena područja
Fizika, Kemija, Biologija

POVEZANOST RADA