Polyarginine Peptides As a New Class of Ligands of Nicotinic Acetylcholine Receptors
Kryukova E. V., Ivanov I. A., Lebedev D. S., Spirova E. N., Senko D. A., Egorova N. S., Kasheverov I. E., Tsetlin V. I.
Doklady Biochemistry and Biophysics
Vol.483, Issue1, P. 313-315
Опубликовано: 2018
Тип ресурса: Статья
DOI:10.1134/S1607672918060017
Аннотация:
Arginine-containing peptides R3, R8, and R16 were obtained by solid-phase peptide synthesis, and their binding to nicotinic acetylcholine receptors (nAChRs) of muscle and neuronal (α7) types was studied by competitive radioligand assay with the use of 125I-α-bungarotoxin. The resulting peptides exhibited a significantly greater binding activity with respect to the muscle-type nAChRs than to the α7 receptor. Thus, we have discovered a new class of nAChR ligands. The affinity of the synthesized oligoarginines for nAChR depended on the number of amino acid residues in the chain. The highest affinity was exhibited by the R16 peptide, which contained 16 arginine residues. © 2018, Pleiades Publishing, Inc.
Ключевые слова:
bungarotoxin receptor; ligand; peptide; polyarginine; animal; chemistry; synthesis; Torpedo; alpha7 Nicotinic Acetylcholine Receptor; Animals; Ligands; Peptides; Torpedo
Язык текста: Английский
ISSN: 1608-3091
Kryukova E. V.
Ivanov I. A.
Lebedev D. S.
Spirova E. N.
Senko D. A.
Egorova N. S.
Kasheverov I. E. Igor` Evgenyevich 1966-
Tsetlin V. I.
Крюкова Е. В.
Иванов И. А.
Лебедев Д. С.
Спирова Е. Н.
Сенко Д. А.
Егорова Н. С.
Кашеверов И. Е. Игорь Евгеньевич 1966-
Цетлин В. И.
Polyarginine Peptides As a New Class of Ligands of Nicotinic Acetylcholine Receptors
Текст визуальный непосредственный
Doklady Biochemistry and Biophysics
Pleiades Publishing, Ltd.
Vol.483, Issue1 P. 313-315
2018
Статья
bungarotoxin receptor ligand peptide polyarginine animal chemistry synthesis Torpedo alpha7 Nicotinic Acetylcholine Receptor Animals Ligands Peptides Torpedo
Arginine-containing peptides R3, R8, and R16 were obtained by solid-phase peptide synthesis, and their binding to nicotinic acetylcholine receptors (nAChRs) of muscle and neuronal (α7) types was studied by competitive radioligand assay with the use of 125I-α-bungarotoxin. The resulting peptides exhibited a significantly greater binding activity with respect to the muscle-type nAChRs than to the α7 receptor. Thus, we have discovered a new class of nAChR ligands. The affinity of the synthesized oligoarginines for nAChR depended on the number of amino acid residues in the chain. The highest affinity was exhibited by the R16 peptide, which contained 16 arginine residues. © 2018, Pleiades Publishing, Inc.