p53 mutant aggregation can result in loss-of-function (LoF), dominant-negative (DN) and gain-of-function (GoF) effects, experiencing tumor growth. Finding inhibition ways of p53 mutant aggregation is really a key step for developing new therapeutics against aggregation-connected cancers. Recent reports have proven that the cell-permeable peptide, ReACp53, can hinder aggregation from the p53 mutant and restore p53 nuclear be the transcriptional factor, showing remarkable therapeutic potential. However, the molecular mechanism underlying the inhibition of p53 mutant aggregation through the ReAp53 peptide is unclear. Within this work, we used all-atom molecular dynamics (MD) simulations to research the result of ReACp53 peptide around the structural and dynamic qualities from the p53 core domain (p53C) from the aggregation-prone R175H mutant. Our simulations says the ReACp53 peptide can stabilize the purchased secondary structure and reduce the versatility of disordered looped the R175H mutant through growing the intra-interactions of p53C. Furthermore, we discovered that ReACp53 peptide particularly binds towards the fragment (residues 180-233) from the R175H mutant through strong hydrophobic interactions with residues L188 and L201 along with a salt bridge or hydrogen bond formation with residues D186, E198, D204, E221 and E224. The particular binding pattern protects the aggregation-prone fragment (residues 182-213) from contact with water. Hence, we recommended the ReACp53 peptide inhibits aggregation from the R175H mutant by restoring nature-type conformation from your aggregation-prone condition and lowering the exposure from the aggregation-prone segment. These results provide molecular mechanistic understanding of inhibition from the ReACp53 peptide on amyloid aggregation from the R175H mutant.ReACp53