Matic Broz (Avtor), Veronika Furlan (Avtor), Samo Lešnik (Avtor), Marko Jukič (Avtor), Urban Bren (Avtor)

Povzetek

Manganese Superoxide Dismutase (MnSOD) represents a mitochondrial protein that scavenges reactive oxygen species (ROS) responsible for oxidative stress. A known single nucleotide polymorphism (SNP) rs4880 on the SOD2 gene, causing a mutation from alanine to valine (Ala16Val) in the primary structure of immature MnSOD, has been associated with several types of cancer and other autoimmune diseases. However, no conclusive correlation has been established yet. This study aims to determine the effect of the alanine to valine mutation on the secondary structure of the MnSOD mitochondrial targeting sequence (MTS). A model for each variant of the MTS was prepared and extensively simulated with molecular dynamics simulations using the CHARMM36m force field. The results indicate that the alanine variant of the MTS preserves a uniform α-helical secondary structure favorable for the protein transport into mitochondria, whereas the valine variant quickly breaks down its α-helix. Thus, the alanine MTS represents the more active MnSOD variant, the benefits of which have yet to be determined experimentally.

Ključne besede

polimorfizmi;dinamika molekul;manganese superoxide dismutase;polymorphism rs4880;mutation Ala16Va;molecular dynamics simulations;oxidative stress;

Podatki

Jezik: Angleški jezik
Leto izida:
Tipologija: 1.01 - Izvirni znanstveni članek
Organizacija: UM FKKT - Fakulteta za kemijo in kemijsko tehnologijo
UDK: 543
COBISS: 131249155 Povezava se bo odprla v novem oknu
ISSN: 2076-3921
Št. ogledov: 34
Št. prenosov: 2
Ocena: 0 (0 glasov)
Metapodatki: JSON JSON-RDF JSON-LD TURTLE N-TRIPLES XML RDFA MICRODATA DC-XML DC-RDF RDF

Ostali podatki

Sekundarni jezik: Slovenski jezik
Sekundarne ključne besede: polimorfizmi;dinamika molekul;polimorfizem rs4880;mutacija Ala16Val;oksidativni stres;
Vrsta dela (COBISS): Znanstveno delo
Strani: 18 str.
Letnik: ǂVol. ǂ11
Zvezek: ǂIss. ǂ12
Čas izdaje: 2022
DOI: 10.3390/antiox11122348
ID: 19829929