چکیده مقاله
The tripeptide Arg Gly Asp acid RGD is a protein sequence in the binding of proteins to cell surfaces, and is involved in various biological processes such as cell adhesion to the extracellular matrix, platelet activation, hemostasis, etc The C2 domain of the Von Willebrand Factor VWF , containing the RGD motif, plays an important role in the initial homeostasis process It binds to the αIIbβ3 integrin and stimulates platelet aggregation We have investigated, using the Molecular Dynamic MD simulation method, the effect of the RGD peptide length, and temperature variation, on the binding to the αIIbβ3 integrin receptor We examined 10 different structural modes of the αIIbβ3 at three different temperatures; 237K, 310K and 318K Our findings show that the amino acids that form a binding pocket include Asp224, Tyr234, Ser226, Tyr190, Tyr189, Trp260, Trp262, Asp259, Lys253, Arg214, Asp217, Ser161 and Ala218 and that the ligand receptor interaction was increased at higher temperatures It was also found that the increase in the number of ligands’ amino acids and their types % glycine plays an important role in the stability, conformation, and ligand receptor interaction
کلیدواژهها
نویسندگان
Hossein Arzani
Department of Medical Physics and Biomedical Engineering, Shahada Behest University of Medical Sciences, Tehran, Iran
Hashem Rafii-Tabar
The Physics Branch of Iran Academy of Sciences
Fatemeh Ramezani
Physiology Research Center, Faculty of Medicine, Iran University of Medical Sciences, Tehran, Iran
شیوه ارجاع
Arzani, Hossein and Rafii-Tabar, Hashem and Ramezani, Fatemeh,1401,The investigation into the effect of the length of RGD peptides and temperature on the interaction with the αIIbβ3 integrin: a molecular dynamic study,International Conference on Leading Research in Nanotechnology Students,Tehran
ارائهشده در
مجموعه مقالات اولین کنفرانس بین المللی تحقیقات پیشرو دانشجویان نانو فناوری30 آبان 1401 · تهران