Chiral Linked Systems as a Model for Understanding D-Amino Acids Influence on the Structure and Properties of Amyloid Peptides |
| |
| Authors: | Aleksandra A Ageeva Alexander B Doktorov Nikolay E Polyakov Tatyana V Leshina |
| |
| Affiliation: | 1.Voevodsky Institute of Chemical Kinetics and Combustion, 630090 Novosibirsk, Russia; (A.A.A.); (N.E.P.); (T.V.L.);2.Department of Natural Sciences, Novosibirsk State University, 630090 Novosibirsk, Russia |
| |
| Abstract: | In this review, we provide an illustration of the idea discussed in the literature of using model compounds to study the effect of substitution of L- for D-amino acid residues in amyloid peptides. The need for modeling is due to the inability to study highly disordered peptides by traditional methods (high-field NMR, X-ray). At the same time, the appearance of such peptides, where L-amino acids are partially replaced by D-analogs is one of the main causes of Alzheimer’s disease. The review presents examples of the use diastereomers with L-/D-tryptophan in model process—photoinduced electron transfer (ET) for studying differences in reactivity and structure of systems with L- and D-optical isomers. The combined application of spin effects, including those calculated using the original theory, fluorescence techniques and molecular modeling has demonstrated a real difference in the structure and efficiency of ET in diastereomers with L-/D-tryptophan residues. In addition, the review compared the factors governing chiral inversion in model metallopeptides and Aβ42 amyloid. |
| |
| Keywords: | chiral linked systems diastereomers D-amino acids amyloid peptides electron transfer chiral inversion spin effects fluorescence quenching molecular dynamics |
|
|
