Alexander Skripnikov

Dr. Alexander Skripnikov


Research Focus & Metrics

Academic Career Length

18Years (2009-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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15 March 2015 in BMC Plant Biology
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IFIgor Fesenko
Igor Fesenko
GAGeorgij Arapidi
Georgij Arapidi
ASAlexander Skripnikov
Alexander Skripnikov
DADmitry G Alexeev
Dmitry G Alexeev
EKElena Kostryukova
Elena Kostryukova
Vadim T. IvanovVadim T. Ivanov
Vadim T. Ivanov
Protein degradation is a basic cell process that operates in general protein turnover or to produce bioactive peptides. However, very little is known about the qualitative and quantitative composition of a plant cell peptidome, the actual result of this degradation. In this study we comprehensively analyzed a plant cell peptidome and systematically analyzed the peptide generation process. We thoroughly analyzed native peptide pools of Physcomitrella patens moss in two developmental stages as well as in protoplasts. Peptidomic analysis was supplemented by transcriptional profiling and quantitative analysis of precursor proteins. In total, over 20,000 unique endogenous peptides, ranging in size from 5 to 78 amino acid residues, were identified. We showed that in both the protonema and protoplast states, plastid proteins served as the main source of peptides and that their major fraction formed outside of chloroplasts. However, in general, the composition of peptide pools was very different between these cell types. In gametophores, stress-related proteins, e.g., late embryogenesis abundant proteins, were among the most productive precursors. The Driselase-mediated protonema conversion to protoplasts led to a peptide generation “burst”, with a several-fold increase in the number of components in the latter. Degradation of plastid proteins in protoplasts was accompanied by suppression of photosynthetic activity. We suggest that peptide pools in plant cells are not merely a product of waste protein degradation, but may serve as important functional components for plant metabolism. We assume that the peptide “burst” is a form of biotic stress response that might produce peptides with antimicrobial activity from originally functional proteins. Potential functions of peptides in different developmental stages are discussed.

11 September 2020 in Molecules
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IZIgor Zlatskiy
Igor Zlatskiy
Tatiana Vadimovna PletenevaTatiana Vadimovna Pleteneva
Tatiana Vadimovna Pleteneva
ASAlexander Skripnikov
Alexander Skripnikov
Tatiana Vladimirovna GrebennikovaTatiana Vladimirovna Grebennikova
Tatiana Vladimirovna Grebennikova
TMTatiana Maksimova
Tatiana Maksimova
ASAnton Syroeshkin
Anton Syroeshkin
The kinetics of biological reactions depends on the deuterium/protium (D/H) ratio in water. In this work, we describe the kinetic model of biocatalytic reactions in living organisms depending on the D/H ratio. We show that a change in the lifetime or other characteristics of the vital activity of some organisms in response to a decrease or increase in the content of deuterium in the environment can be a sign of a difference in taxons. For animals—this is a curve with saturation according to the Gauss’s principle, for plants—it is the Poisson dependence, for bacteria a weakly saturated curve with a slight reaction to the deuterium/protium ratio toward increasing deuterium. The biological activity of the aquatic environment with reduced, elevated, and natural concentrations of deuterium is considered. The results of the study are presented in different vital indicators of some taxons: the bacteria kingdom—the colony forming units (CFU) index (Escherichia coli); animals—the activation energy of the death of ciliates (Spirostomum ambiguum), embryogenesis of fish (Brachydanio rerio); plants—germination and accumulation of trace elements Callisia fragrans L., sprouting of gametophores and peptidomics of moss Physcomitrella patens. It was found that many organisms change their metabolism and activity, responding to both high and low concentrations of deuterium in water.

1 January 2011 in Russian Journal of Bioorganic Chemistry
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Journal Article
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ASAlexander Skripnikov
Alexander Skripnikov
NAN. A. Anikanov
N. A. Anikanov
VKV. S. Kazakov
V. S. Kazakov
SDS. V. Dolgov
S. V. Dolgov
RZR. Kh. Ziganshin
R. Kh. Ziganshin
VIV. T. Ivanov
V. T. Ivanov
The isolation and identification of peptides from the moss Physcomitrella patens (Hedw.) B.S.G., which has been widely used in recent years as a model for studying plant biology, has been described. It was shown for the first time that protoplasts, the protonemata, and gametophores of Ph. patens contain a variety of peptides. From gametophores, 58 peptides, which are the fragments of 14 proteins, and from the protonemata, 49 peptides, the fragments of 15 proteins, were isolated and identified. It was found that the protonemata and gametophores of Ph. patens, which are the successive stages of the development of this plant, significantly differ from each other in both the peptide composition and the spectrum of precursor proteins of the identified peptides. The isolation of protoplasts during the enzymatic destruction of the protonema cell wall is accompanied by massive degradation of intracellular proteins, many of which are the proteins of the protosynthetic system, which is a characteristic response of higher plants to environmental stress factors. In all, 323 peptides, which are the fragments of 79 proteins, were isolated and identified from moss protoplasts.

24 May 2009 in Biochemistry (Moscow)
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ASAlexander Skripnikov
Alexander Skripnikov
NPNikita Polyakov
Nikita Polyakov
ETE. V. Tolcheva
E. V. Tolcheva
VVV. V. Velikodvorskaya
V. V. Velikodvorskaya
SDS. V. Dolgov
S. V. Dolgov
VGV. M. Govorun
V. M. Govorun
The sequencing of the moss Physcomitrella patensgenome has facilitated studies of the plant proteome. To develop a proteome reference map based on the genome sequence, we conducted 2D...