Unveiling　the　self-assembly　mechanism　of　amphiphilic　peptides　is　crucial　for　the　development　of　functional　supramolecular　biomaterials.　The　chemical　properties　of　hydrophilic　amino　acids　play　an　essential　role　in　this　process.　Our　multiscale　molecular　dynamics　(MD)　simulations　indicated　that　the　hydrophilic　residue,　threonine　(T),　is　an　excellent　candidate　to　balance　the　hydrophobicity　of　the　peptide,　which　could　enhance　the　self-assembly　ability　of　the　peptide.　In　addition,　simulations　demonstrated　that　the　number　of　hydrogen　bonds　within　peptide　assemblies　did　not　correlate　directly　with　their　stability.　Preventing　hydrophilic　side　chains　from　disrupting　the　hydrogen　bond　network　between　the　peptide　backbones　can　improve　self-assembly　stability.　Together　with　the　experimental　validation,　we　believe　that　T　is　a　promising　amino　acid　to　balance　the　hydrophobicity　of　amphiphilic　peptides.　This　work　highlights　the　importance　of　hydrophilic　amino　acids　in　peptide　self-assembly,　which　could　be　further　utilized　for　designing　amphiphilic　peptides　with　different　functions.