Novel RGD-containing peptides exhibited improved abilities to integrin receptor binding and cultures of human induced pluripotent stem cells.

[Display omitted] • Design novel peptides from the nearing aspartic acid sequence of two reported Arg-Gly-Asp (RGD)-containing peptides. • Improve the ability of peptides in the culture of human induced pluripotent stem cells. • The mechanism underlies peptide sequence-induced cell culture ability is revealed in detail. • The high affinity between peptides and corresponding integrin receptors positively correlates to its ability in cell culture. The design of novel peptide sequences and investigations of the mechanisms underlying cell adhesion is critical for the culture of human induced pluripotent stem cells (hiPSCs) on the peptide displaying surfaces. Recently, we reported that near-Asp sequences play an important role in the function of whole Arg-Gly-Asp (RGD)-containing peptides. In this study, two novel peptides with sequences of Ac-KGGTYRAYRGDVFTMP and Ac-KGGVFTMPRGDTYRAY were designed from reported peptides. Fortunately, the Ac-KGGVFTMPRGDTYRAY peptide exhibited excellent ability in sustaining cultures of hiPSCs. Moreover, we predicted the structural model of peptides by molecular dynamics simulation and successfully obtained the complex structure of peptides and αVβ3/αVβ5 integrin proteins through molecular docking. Finally, a strong affinity to the αVβ3 integrin receptor contributes to the excellent ability of peptide was confirmed. Study reveals the mechanisms by which RGD-containing peptides support the adhesion and provides a better peptide for hiPSCs culture. [ABSTRACT FROM AUTHOR]