Chiral Linked Systems as a Model for Understanding D-Amino Acids Influence on the Structure and Properties of Amyloid Peptides

Standard

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. et al.

In: International Journal of Molecular Sciences, Vol. 23, No. 6, 3060, 01.03.2022.

Research output: Contribution to journal › Review article › peer-review

BibTeX

@article{a1a6b2c05382492f9abd0b1a687752c6,

title = "Chiral Linked Systems as a Model for Understanding D-Amino Acids Influence on the Structure and Properties of Amyloid Peptides",

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{\textquoteright}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 = "Amyloid peptides, Chiral inversion, Chiral linked systems, D-amino acids, Diastereomers, Electron transfer, Fluorescence quenching, Molecular dynamics, Spin effects",

author = "Ageeva, {Aleksandra A.} and Doktorov, {Alexander B.} and Polyakov, {Nikolay E.} and Leshina, {Tatyana V.}",

note = "Funding Information: Funding: This research was funded by Russian Science Foundation, grant number 18-13-00047. Publisher Copyright: {\textcopyright} 2022 by the authors. Licensee MDPI, Basel, Switzerland.",

year = "2022",

month = mar,

day = "1",

doi = "10.3390/ijms23063060",

language = "English",

volume = "23",

journal = "International Journal of Molecular Sciences",

issn = "1661-6596",

publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",

number = "6",

}

RIS

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.

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