Результаты исследований: Научные публикации в периодических изданиях › обзорная статья › Рецензирование
Chiral Linked Systems as a Model for Understanding D-Amino Acids Influence on the Structure and Properties of Amyloid Peptides. / Ageeva, Aleksandra A.; Doktorov, Alexander B.; Polyakov, Nikolay E. и др.
в: International Journal of Molecular Sciences, Том 23, № 6, 3060, 01.03.2022.Результаты исследований: Научные публикации в периодических изданиях › обзорная статья › Рецензирование
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TY - JOUR
T1 - Chiral Linked Systems as a Model for Understanding D-Amino Acids Influence on the Structure and Properties of Amyloid Peptides
AU - Ageeva, Aleksandra A.
AU - Doktorov, Alexander B.
AU - Polyakov, Nikolay E.
AU - Leshina, Tatyana V.
N1 - Funding Information: Funding: This research was funded by Russian Science Foundation, grant number 18-13-00047. Publisher Copyright: © 2022 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2022/3/1
Y1 - 2022/3/1
N2 - 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.
AB - 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.
KW - Amyloid peptides
KW - Chiral inversion
KW - Chiral linked systems
KW - D-amino acids
KW - Diastereomers
KW - Electron transfer
KW - Fluorescence quenching
KW - Molecular dynamics
KW - Spin effects
UR - http://www.scopus.com/inward/record.url?scp=85126089092&partnerID=8YFLogxK
UR - https://www.mendeley.com/catalogue/d7e73c1a-111b-36cb-bb4e-232e89316411/
U2 - 10.3390/ijms23063060
DO - 10.3390/ijms23063060
M3 - Review article
C2 - 35328481
AN - SCOPUS:85126089092
VL - 23
JO - International Journal of Molecular Sciences
JF - International Journal of Molecular Sciences
SN - 1661-6596
IS - 6
M1 - 3060
ER -
ID: 35689838