Conformation Analysis of Peptides Derived from Laminin Alpha 1–2 Chain Using Molecular Dynamics Simulation

Laminin is one of the components of the basement membrane and, laminin has diverse biological activities [1-2], such as promotion of cell attachment, cell migration, tumor metastasis, neurite outgrowth and angiogenesis [2]. Previously, Suzuki et al. identified several functional peptides (EF1-EF5) derived from LG4 modules of laminin alpha 1-5 chains [3]. Previous results showed that biological activities of N-terminal and C-terminal truncated peptide of EF1 are enhanced by disulfide bond [3], and the importance of hairpin-like structure was suggested. By contrast, the EF2 does not have biological activity despite the homologous sequence of the EF1 [4]. Based on these results, the relationship between conformation and activity can be suggested. Thus, we perform conformation analysis of EF1 and EF2 using molecular dynamics simulations.