Novel Inhibitors for Allosteric Site 2 of SHP 2 Enzyme Based on Natural Organic Compounds: A Rational In Silico design

inhibition of SHP 2(a cytoplasmic protein tyrosine phosphatase) phosphatase) activity was reported as potential immunotherapy and cancer treatment; because of its role in cell proliferation, differentiation, survival and numerous oncogenic signaling cascades. due to the challenges of SHPSHP 2 active site inhibition like its highly conserved, polar, charged environment, scientific researches have focused on inhibition through the allosteric site of the enzyme. SHP 099 as a high aqueous soluble, selective, and oral bioavailable compound binds to the tunnel like allosteric site 1of the enzyme and inhibit SHP 2action through stabilizing it in its autoinhibited conformation Recently anew allosteric site have been discovered and through investigations to discover structures to inhibit enzyme by allosteric site 2,SHP 244 has identified. Combining an allosteric site 1inhibitor with an allosteric site 2inhibitor inhibitor led to enhanced pharmacological pathway inhibition in cells. Utilizing Peptides as therapeutic agents for cancertherapy, bring lots of advantages like easily modification, rapid Synthesis, being atoxic. Among peptide family, dipetide have show inhibitory effect on allosteric site 1. Also, Glycosylation is an important parameter in the optimization of many peptide drugs This work is an in silico effort to introduce novel structures for allosteric site 2 inhibition which have amino acids and monosaccharides segments.