Investigation of structural properties of lunasin with computational tools

سال انتشار: 1400
نوع سند: مقاله کنفرانسی
زبان: انگلیسی
مشاهده: 135

نسخه کامل این مقاله ارائه نشده است و در دسترس نمی باشد

این مقاله در بخشهای موضوعی زیر دسته بندی شده است:

استخراج به نرم افزارهای پژوهشی:

لینک ثابت به این مقاله:

شناسه ملی سند علمی:

IBIS10_263

تاریخ نمایه سازی: 5 تیر 1401

چکیده مقاله:

Lunasin is a soy-derived chemical that slows the proliferation of newly identified cancer cells. Thissubstance's anti-cancer properties have gotten increased attention .In the treatment of disorders, lunasin hasbeen found to have cholesterol-lowering and hypertensive effects. Lunasin is a ۴۳-amino-acid peptide havinga SKWQHQQDSCRKQLQGVNLTPCEKHIMEKIQGRGDDDDDDDDD sequence and a molecularweight of ۵.۵ KDa .Tumor cells can adhere to the extracellular matrix due to the RGD motif found in lunasin.In fact, by fighting for adhesion, the peptides in this motif can suppress cancer.The properties of lunacin were investigated using computational tools using bioinformatics tools. The secondstructure of lunasin was derived using the database http://cib.cf.ocha.ac.jp/bitool/MIX, then its third structurewas analyzed utilizing the ITASSER database due to laboratory restrictions and the tiny size of this sequence.Its structure is seen using the Spdb viewer software. The Co - factor server was used to find the peptide'sfunctional area. The hotspot wizard server looked at possible locations for examining mutations in thestructure of lunasin. It was tested utilizing a prosper site and a peptide cutter to make greater utilization ofenzymes. The anticp database was used to investigate cancer qualities, as well as other ACPHP properties.The amino acids S۱, R۱, R۳, T۳, K۲, K۲۴, K۲۹, K۱۲, and D۱۸ from the region that plays a role in stabilitycan be altered, however the functional region cannot. The results revealed that this peptide possesses anticancercapabilities, with KHIMG receiving the highest score of ۸۷%. QGRGDDDDDD has also beendiscovered to have antihypertensive characteristics, with an ۸۱ percent score. CNBr enzymes were found tobe capable of selective cleavage of the lunasin peptide Chymotripsine, Clostripain.

نویسندگان

Fatemeh Safakhah

Biotechnology Group, Al-Zahra University, Tehran, Iran

Mahboobeh Zarrabi

Biotechnology Group, Al-Zahra University, Tehran, Iran

Fakhri Sadat Hoseyni

Biotechnology Group, Al-Zahra University, Tehran, Iran