TY - JOUR

T1 - Role of chiral configuration in the photoinduced interaction of d-and l-tryptophan with optical isomers of ketoprofen in linked systems

AU - Ageeva, Aleksandra A.

AU - Magin, Ilya M.

AU - Doktorov, Alexander B.

AU - Plyusnin, Victor F.

AU - Kuznetsova, Polina S.

AU - Stepanov, Alexander A.

AU - Alekseev, Alexander A.

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: © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

PY - 2021/6/2

Y1 - 2021/6/2

N2 - The study of the L-and D-amino acid properties in proteins and peptides has attracted considerable attention in recent years, as the replacement of even one L-amino acid by its D-analogue due to aging of the body is resulted in a number of pathological conditions, including Alzheimer’s and Parkinson’s diseases. A recent trend is using short model systems to study the peculiarities of proteins with D-amino acids. In this report, the comparison of the excited states quenching of Land D-tryptophan (Trp) in a model donor–acceptor dyad with (R)-and (S)-ketoprofen (KP-Trp) was carried out by photochemically induced dynamic nuclear polarization (CIDNP) and fluorescence spectroscopy. Quenching of the Trp excited states, which occurs via two mechanisms: prevailing resonance energy transfer (RET) and electron transfer (ET), indeed demonstrates some peculiarities for all three studied configurations of the dyad: (R,S)-, (S,R)-, and (S,S)-. Thus, the ET efficiency is identical for (S,R)-and (R,S)-enantiomers, while RET differs by 1.6 times. For (S,S)-, the CIDNP coefficient is almost an order of magnitude greater than for (R,S)-and (S,R)-. To understand the source of this difference, hyperpolarization of (S,S)-and (R,S)-has been calculated using theory involving the electron dipole–dipole interaction in the secular equation.

AB - The study of the L-and D-amino acid properties in proteins and peptides has attracted considerable attention in recent years, as the replacement of even one L-amino acid by its D-analogue due to aging of the body is resulted in a number of pathological conditions, including Alzheimer’s and Parkinson’s diseases. A recent trend is using short model systems to study the peculiarities of proteins with D-amino acids. In this report, the comparison of the excited states quenching of Land D-tryptophan (Trp) in a model donor–acceptor dyad with (R)-and (S)-ketoprofen (KP-Trp) was carried out by photochemically induced dynamic nuclear polarization (CIDNP) and fluorescence spectroscopy. Quenching of the Trp excited states, which occurs via two mechanisms: prevailing resonance energy transfer (RET) and electron transfer (ET), indeed demonstrates some peculiarities for all three studied configurations of the dyad: (R,S)-, (S,R)-, and (S,S)-. Thus, the ET efficiency is identical for (S,R)-and (R,S)-enantiomers, while RET differs by 1.6 times. For (S,S)-, the CIDNP coefficient is almost an order of magnitude greater than for (R,S)-and (S,R)-. To understand the source of this difference, hyperpolarization of (S,S)-and (R,S)-has been calculated using theory involving the electron dipole–dipole interaction in the secular equation.

KW - Chiral linked systems

KW - Diastereomers

KW - Electron transfer

KW - Enantiomers

KW - Magnetic dipole–dipole interaction of electrons

KW - Resonance energy transfer

KW - Stereoisomerism

KW - Ketoprofen/chemistry

KW - Tryptophan/chemistry

KW - Molecular Structure

KW - Energy Transfer

KW - Photochemistry

UR - http://www.scopus.com/inward/record.url?scp=85107367526&partnerID=8YFLogxK

U2 - 10.3390/ijms22126198

DO - 10.3390/ijms22126198

M3 - Article

C2 - 34201293

AN - SCOPUS:85107367526

VL - 22

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1661-6596

IS - 12

M1 - 6198

ER -