ИССЛЕДОВАНИЕ АФФИННОСТИ ВЗАИМОДЕЙСТВИЯ ПРОИЗВОДНЫХ РЕКОМБИНАНТНОГО АНТИМЮЛЛЕРОВА ГОРМОНА ЧЕЛОВЕКА С РЕКОМБИНАНТНЫМ РЕЦЕПТОРОМ II ТИПА.

А.Я. Рак, А.В. Трофимов, Н.П. Горбунов, А.В. Соколов

Research output: Contribution to conferenceAbstract

Abstract

To date, human recombinant anti-mullerian hormone (rAMH) is considered to be a basis of new targeted antitumor drug. Its development is largely hampered by the lack of information about the mechanism of rAMH and its derivatives interaction with a specific type II receptor (MISRII). Here, the surface plasmon resonance method was used to study the affinity of rAMH and its derivatives binding to the recombinant MISRII analogue. The affinity of three hormone derivatives interaction with MISRII turned out to be signifi cantly different. C-rAMH binding to the receptor was characterized by maximum affinity (was estimated by the values of the equilibrium dissociation constant KD, the association constant ka and the dissociation rate constant kd). At the same time, the prohormone affinity to the receptor was 40 times lower than that of C-rAMH, but slightly higher than that of the half-cleaved rAMH form. The results indicate the highest affinity of C-rAMH interaction with MISRII and consequent
Original languageRussian
Pages587-590
StatePublished - 2019
Externally publishedYes

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