Journal
JOURNAL OF MOLECULAR GRAPHICS & MODELLING
Volume 84, Issue -, Pages 145-151Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jmgm.2018.06.012
Keywords
PAMAM dendrimer; G-actin; Molecular dynamics; Adsorption
Categories
Funding
- NSFC [21474074, 21674078, 21574096, 21774091, 21374073]
- National Science Foundation of China (NSFC)
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Understanding the interactions of dendrimers as drug/gene delivery vectors with proteins is important for functional optimization. Here, atomistic molecular dynamics simulations are employed to study the interactions between six positively-charged polyamidoamine dendrimers of the second generation (G2 PAMAM) and G-actin. We find that the structure of G-actin is relatively stable after dendrimers' binding. PAMAM dendrimers also do not significantly change the secondary structure of G-actin. Furthermore, we find the formation of dendrimer-actin complex is mainly driven by electrostatic interactions. Moreover, we suggest the secondary structure change of local domains of G-actin is probably responsible to the inhibition of actin polymerization. (C) 2018 Elsevier Inc. All rights reserved.
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