Zwitterionic dendrimer is an effective carrier, which can restore the natural conformation of peptide segments for high bioaffinity by a hydrogen bond-induced conformational constraint approach. However, it is still unknown whether the approach is applicable for the dendrimers with different geometric sizes. Therefore, the characteristics of conjugates made from zwitterionic poly(amidoamine) (PAM) and the arginine-glycine-aspartic acid (RGD) peptide were examined to elucidate the effects of the geometric sizes of the PAM dendrimer on the conformational structure and stability of the peptide. The results show that the RGD fragments had almost the same structure and stability when conjugated with PAM(G3, G4, or G5) dendrimers. However, when conjugated with PAM(G1 or G2) dendrimers, the structural stability of these fragments was found to be much worse. Also, the structure and stability of RGD segments conjugated with PAM(G3, G4, or G5) were not affected when additional EK segments were inserted. Moreover, we observed that RGD fragments conjugated with PAM(G3, G4, or G5) dendrimers were structurally stable and similar when the concentration of NaCl was 0.15 and 0.5M. Furthermore, we show that PAM(G3, G4, or G5)-RGD conjugates bind strongly to integrin αvβ3.
Molecular simulation studies on a zwitterionic peptide-dendrimer conjugate for integrin αvβ3 binding
Note: This paper is part of the Biointerphases Special Topic Collection on Biointerface Science in China.
Xiaowei Lin, Nan Xu, Chen Li, Zhiyu Wu, Shengfu Chen, Yao Shi, Yi He; Molecular simulation studies on a zwitterionic peptide-dendrimer conjugate for integrin αvβ3 binding. Biointerphases 1 May 2023; 18 (3): 031004. https://doi.org/10.1116/6.0002713
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