Equilibrium and non-equilibrium aggregation in the model peptide family AnX
Başlık çevirisi mevcut değil.
- Tez No: 540032
- Danışmanlar: Prof. ULF OLSSON
- Tez Türü: Doktora
- Konular: Biyofizik, Biyomühendislik, Kimya, Biophysics, Bioengineering, Chemistry
- Anahtar Kelimeler: Belirtilmemiş.
- Yıl: 2013
- Dil: İngilizce
- Üniversite: Lunds Universitet
- Enstitü: Yurtdışı Enstitü
- Ana Bilim Dalı: Belirtilmemiş.
- Bilim Dalı: Belirtilmemiş.
- Sayfa Sayısı: 68
Özet
Özet yok.
Özet (Çeviri)
The object of this thesis was to investigate how minor changes in the amino acid sequence of a small model peptide affected the self-assembly behavior. The self-assembled structures of synthetic peptides, AnX where A is alanine, X can be lysine (K), arginine (R) or aspartic acid (D), and n is the number of alanine residues in the sequence were investigated. The aggregates were characterized by Small Angle X-ray Scattering (SAXS), Static (SLS) and Dynamic (DLS) Light Scattering, Cryogenic Transmission Electron Microscopy (Cryo- TEM), Circular Dichroism (CD) and Fourier Transform Infra Red Spectroscopy (FTIR). It was shown that the combined studies of time resolved SAXS and Cryo-TEM were useful not only the physical characterization of the aggregates but also in the elucidation of formation and dissolution processes. A particular effort was given to assess the thermodynamic stability of the aggregates. Taking the A6K-water system as a basis, effects of hydrophobic and electrostatic interaction on peptide self-assembly were studied. By increasing n, for AnK-water systems, the effect of hydrophobicity was investigated. Increasing the number of hydrophobic alanine residues has a strong effect on the aqueous peptide solubility. The solubility decreases approximately by an order of magnitude for each additional alanine residue. n also affects the preferred aggregate shape. Effects of charge distribution were studied by exchanging the positively charged amino acid (K) with a negatively charged amino acid (D). Furthermore, while maintaining the overall charge, the sensitivity of peptide self-assembly to small changes in the side chain was tested by exchanging K with R. We conclude that peptide self-assembly is very sensitive to the small changes in the amino acid sequence. Based on the results from this thesis, small changes in the peptide sequence can result in aggregates that are either equilibrium or nonequilibrium structures. Key words peptides, self-assembly, nanotubes, SAXS/WAXS, phase behavior
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