期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 113, 期 19, 页码 6986-6993出版社
AMER CHEMICAL SOC
DOI: 10.1021/jp9011119
关键词
-
资金
- Natural Sciences and Engineering Research Council of Canada (NSERC)
- Missouri State University
Dendrimers are synthetic, highly branched, spherical macromolecules with nanometer dimensions and potential applications in DNA and drug delivery systems. Human serum albumin (HSA) is a major transporter for delivering several endogenous compounds and drugs in vivo. The aim of this study was to examine the interaction of human serum albumin with several dendrimers such as mPEG-PAMAM (Q3), mPEG-PAMAM (G4), and PAMAM (G4) at physiological conditions, using constant protein concentration and various dendrimer compositions. FTIR, UV-visible, CD, and fluorescence spectroscopic methods were used to analyze macromolecule binding mode, the binding constant and the effects of dendrimers complexation on HSA stability and conformation. Structural analysis showed that dendrimers bind HSA via polypeptide polar groups (hydrophilic) with number of bound polymer (n) 1.08 (mPEG-PAMAM-G3), 1.50 (mPEG-PAMAM-G4), and 0.96 (PAMAM-G4). The overall binding constants estimated were of KmPEG-G3 = 1.3 (+/-0.2) x 10(4) M-1, KmPEG-G4 = 2.2 (+/-0.4) x 10(4) M-1, and KPAMAM-G4 = 2.6 (+/-0.5) x 10(4) M-1. HSA conformation was altered by dendrimers with a major reduction of alpha-helix and increase in random coil and turn structures suggesting a partial protein unfolding.
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