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

Materials & Design

Feng Lan¹  Fang Feng²  Huanxiang Liu³  Zerong Xu⁴  Jiamin Shi⁴  Fei He⁵  Rongzhi Zhang⁵  Yu Han⁵  Liying Qin⁵  Yameng Song⁵  Jing Li⁵  Qin Li⁵  Hongjiao Li⁵  Ping Zhou⁵ 

[1] Corresponding authors.;Lanzhou University Second Hospital, Lanzhou University, Lanzhou, China;Lanzhou University Second Hospital, Lanzhou University, Lanzhou, China;School of Pharmacy, Lanzhou University, Lanzhou, China;School of Stomatology, Lanzhou University, No.222 Tianshui South Road, Chengguan District, Lanzhou 730000, PR China;

关键词: Human induced pluripotent stem cells;    Synthetic substrate;    Peptides;    RGD sequence;    Integrin receptor;   

DOI  :  

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown