Od białek amyloidogennych do nanostruktur tworzonych przez proste peptydy

Rożniakowski, K. K.; Kamiński, Z. J.

Artykuł - szczegóły

Tytuł artykułu

Od białek amyloidogennych do nanostruktur tworzonych przez proste peptydy

Autorzy

Rożniakowski K. K. , Kamiński Z. J.

Wybrane pełne teksty z tego czasopisma

Identyfikatory

Warianty tytułu

From amyloidogenic proteines to nanostructures formed by simple peptides

Języki publikacji

Abstrakty

Molecular self-assembly offers unique opportunity for the fabrication of novel supramolecular structures and advanced materials. The inspiration for the development of such structures is often resulting from self-assembling modules in biology, as natural systems always form complex structures from relatively simple building blocks [1, 2]. Several studies had demonstrated the versatility of peptide to form well organized assemblies. This includes cyclic peptides designed with alternating D- and L-amino acids, amphiphile peptides, peptide-conjugates and ionic self-complementary peptides. The 37-residue amylin (Fig. 5), also known as islet amyloid polypeptide, forms fibrils that are the main component of amyloid that develops in the pancreas of type 2 diabetes patients. Amylin also in vitro readily forms amyloid fibrils that are highly polymorphic under typical experimental conditions [21-33]. The molecular structure of amylin protofilaments in striated ribbons closely resembles the protofilament in amyloid fibrils with a similar morphology formed by the 40-residue beta-amyloid peptide that is associated with Alzheimer's disease [48-54]. But not only amylin is a self-assembling peptide. We can also find another examples in biological proteins and peptides that have the intrinsic ability to selfassemble into elongated solid nanofibrils, which may give rise to amyloid diseases or alternatively, inspire applications ranging from tissue engineering to nanoelectronics (Fig. 4). Proteinaceous fibrils are extensively studied searching for detailed theoretical models explaining the mechanism of formation, morphology and properties of self-assembled structures. Especially intriguing state of protein-like selfassemblies are nanotubes (NTs), defined as an elongated nano-object with a definite inner hole. In contrast to proteinaceous fibrils, nanotubes are much less frequently observed and far less well understood. However, they have attracted research interest as key components for nanotechnology (Fig. 13). The simplest objects prone to self-assembly are aromatic dipeptides diphenylalanine, diphenylglycine, and their simple derivatives form nanotubes or spherical nanometric assemblies. Remarkable flexibilities of peptides fragments in formation of nanostructures recently have been considered important for many applications in various fields including molecular electronics, tissue engineering, and material science [87-92].

Słowa kluczowe

ß-amyloid amylina samoorganizacja peptyd nanotechnologia

ß-amyloid amylin self-assembling peptide nanotechnology

Wydawca

Polskie Towarzystwo Chemiczne

Czasopismo

Wiadomości Chemiczne

Rocznik

2010

Tom

[Z] 64, 7-8

Strony

645--671

Opis fizyczny

Bibliogr. 92 poz., rys., tab., wykr.

Twórcy

autor

Rożniakowski K. K.

autor

Kamiński Z. J.

Instytut Chemii Organicznej Politechniki Łódzkiej, ul. Żeromskiego 116, 90-924 Łódź, zbigniew.kaminski@p.lodz.pl

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Bibliografia

Identyfikator YADDA

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