Effects of poly(amidoamine) dendrimers on the structure and function of key blood components

Journal of Bioactive and Compatible Polymers

Volumn 29, Issue 2, 2014, Pages 165-179

  Fu, Yeyun ^a   Hu, Rushan ^a   Li, Chenghua ^a   Wang, Qian ^b   Liu, Zonghua ^a   Xue, Wei ^a  

^a JINAN UNIVERSITY   (China)

^b SHANDONG UNIVERSITY   (China)

Author keywords

fibrinogen; hemocompatibility; Poly(amidoamine) dendrimer; red blood cells

Indexed keywords

BIOMEDICAL APPLICATIONS; CONFORMATIONAL CHANGE; FIBRINOGEN; HEMOCOMPATIBILITY; MORPHOLOGICAL CHANGES; POLYAMIDOAMINE DENDRIMERS; RED BLOOD CELL; SURFACE FUNCTIONAL GROUPS;

BLOOD; CATIONIC POLYMERIZATION; CELLS; COAGULATION; DENDRIMERS; FUNCTIONAL GROUPS; MEDICAL APPLICATIONS;

FUNCTIONAL POLYMERS;

DENDRIMER; FIBRINOGEN; FUNCTIONAL GROUP; POLYAMIDOAMINE; POLYAMIDOAMINE DENDRIMER; UNCLASSIFIED DRUG;

ARTICLE; BLOOD CLOTTING; BLOOD COMPONENT; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ERYTHROCYTE AGGREGATION; ERYTHROCYTE STRUCTURE; HEMOLYSIS; HUMAN; HUMAN CELL; POLYMERIZATION; PROTEIN POLYMERIZATION; SURFACE PROPERTY;

EID: 84896712395     PISSN: 08839115     EISSN: 15308030     Source Type: Journal    
DOI: 10.1177/0883911514521921     Document Type: Article

References (24)

1. Pan G, Lemmouchi Y, Akala EO, et al. Studies on PEGylated and drug-loaded PAMAM dendrimers. J Bioact Compat Pol. 2005 ; 20: 113-128
2. Franchini J, Ferruti P. Perspectives on: recent advances in poly(amidoamine)s chemistry. J Bioact Compat Pol. 2004 ; 19: 221-236
3. Jevprasesphant R, Penny J, Jalal R, et al. The influence of surface modification on the cytotoxicity of PAMAM dendrimers. Int J Pharm. 2003 ; 252: 263-266
4. El-Sayed M, Ginski M, Rhodes CA, et al. Influence of surface chemistry of poly(amidoamine) dendrimers on Caco-2 cell monolayers. J Bioact Compat Pol. 2003 ; 18: 7-22
5. Roberts JC, Bhalgat MK, Zera RT. Preliminary biological evaluation of polyamidoamine (PAMAM) Starburst dendrimers. J Biomed Mater Res. 1996 ; 30: 53-65
6. Han MH, Chen J, Wang J, et al. Blood compatibility of polyamidoamine dendrimers and erythrocyte protection. J Biomed Nanotechnol. 2010 ; 6: 82-92
7. Wang W, Xiong W, Zhu Y, et al. Protective effect of PEGylation against poly(amidoamine) dendrimer-induced hemolysis of human red blood cells. J Biomed Mater Res B. 2010 ; 93: 59-64
8. Jones CF, Campbell RA, Franks Z, et al. Cationic PAMAM dendrimers disrupt key platelet functions. Mol Pharm. 2012 ; 9: 1599-1611
9. Jones CF, Campbell RA, Brooks AE, et al. Cationic PAMAM dendrimers aggressively initiate blood clot formation. ACS Nano. 2012 ; 6: 9900-9910
10. Dobrovolskaia MA, Patri AK, Potter TM, et al. Dendrimer-induced leukocyte procoagulant activity depends on particle size and surface charge. Nanomedicine: UK. 2012 ; 7: 245-256
11. Dobrovolskaia MA, Patri AK, Simak J, et al. Nanoparticle size and surface charge determine effects of PAMAM dendrimers on human platelets in vitro. Mol Pharm. 2012 ; 9: 382-393
12. Klajnert B, Pikala S, Bryszewska M. Haemolytic activity of polyamidoamine dendrimers and the protective role of human serum albumin. P Roy Soc A: Math Phy. 2010 ; 466: 1527-1534
13. Ziemba B, Matuszko G, Bryszewska M, et al. Influence of dendrimers on red blood cells. Cell Mol Biol Lett. 2012 ; 17: 21-35
14. Domanski DM, Klajnert B, Bryszewska M. Influence of PAMAM dendrimers on human red blood cells. Bioelectrochemistry. 2004 ; 63: 189-191
15. Ciolkowski M, Rozanek M, Szewczyk M, et al. The influence of PAMAM-OH dendrimers on the activity of human erythrocytes ATPases. BBA: Biomembranes. 2011 ; 1808: 2714-2723
16. Klajnert B, Sadowska M, Bryszewska M. The effect of polyamidoamine dendrimers on human erythrocyte membrane acetylcholinesterase activity. Bioelectrochemistry. 2004 ; 65: 23-26
17. Zhong D, Jiao Y, Zhang Y, et al. Effects of the gene carrier polyethyleneimines on structure and function of blood components. Biomaterials. 2013 ; 34: 294-305
18. Li C, Zhong D, Zhang Y, et al. The effect of the gene carrier material polyethyleneimine on the structure and function of human red blood cells in vitro. J Mater Chem B Mater Biol Med. 2013 ; 1: 1885-1893
19. Zhang W, Zhong D, Liu Q, et al. Effect of chitosan and carboxymethyl chitosan on fibrinogen structure and blood coagulation. J Biomat Sci: Polym E. 2013 ; 24: 1549-1563
20. Shcharbin D, Janicka M, Wasiak M, et al. Serum albumins have five sites for binding of cationic dendrimers. BBA: Proteins Proteom. 2007 ; 1774: 946-951
21. Klajnert B, Stanisławska L, Bryszewska M, et al. Interactions between PAMAM dendrimers and bovine serum albumin. BBA: Proteins Proteom. 2003 ; 1648: 115-126
22. Aggarwal P, Hall JB, McLeland CB, et al. Nanoparticle interaction with plasma proteins as it relates to particle biodistribution, biocompatibility and therapeutic efficacy. Adv Drug Deliver Rev. 2009 ; 61: 428-437
23. Peng HT. Thromboelastographic study of biomaterials. J Biomed Mater Res B. 2010 ; 94: 469-485
24. Petroianu GA, Liu J, Maleck WH, et al. The effect of In vitro hemodilution with gelatin, dextran, hydroxyethyl starch, or Ringer's solution on Thrombelastograph. Anesth Analg. 2000 ; 90: 795-800