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Polyethyleneimine-protein interactions and implications on protein stability

Mazzaferro, Laura; Breccia, Javier D.; Andersson, Maria LU ; Hitzmann, Bernd and Hatti-Kaul, Rajni LU (2010) In International Journal of Biological Macromolecules 47(1). p.15-20
Abstract
Protein stability assessment of seven model proteins in the presence of low molecular weight polyethyleneimine (PEI, MW 2000 Da) was performed. Thermodynamic stability, monitored by circular dichroism (CD) spectroscopy, showed that the polymer did not have a major effect on the melting temperature (T-m) of the basic proteins - muscle lactate dehydrogenase (LDH), ribonuclease A, lysozyme and cutinase, while for the acidic ones - human growth hormone, human serum albumin and heart lactate dehydrogenase - there was a shift in T-m towards lower temperatures. The secondary structures of the basic proteins were essentially the same, with none or a slight increase in the CD spectra, in presence of the polymer. In the case of the acidic proteins,... (More)
Protein stability assessment of seven model proteins in the presence of low molecular weight polyethyleneimine (PEI, MW 2000 Da) was performed. Thermodynamic stability, monitored by circular dichroism (CD) spectroscopy, showed that the polymer did not have a major effect on the melting temperature (T-m) of the basic proteins - muscle lactate dehydrogenase (LDH), ribonuclease A, lysozyme and cutinase, while for the acidic ones - human growth hormone, human serum albumin and heart lactate dehydrogenase - there was a shift in T-m towards lower temperatures. The secondary structures of the basic proteins were essentially the same, with none or a slight increase in the CD spectra, in presence of the polymer. In the case of the acidic proteins, the CD spectra were diminished mostly due to phase separation. Assuming a homogeneous distribution of the net charge on the protein surface a quantitative inverse relationship was established between surface charge density of the acidic proteins and the PEI2000 concentration required for maximum flocculation. Despite lowering the thermal stability of acidic proteins, PEI2000 was seen to protect heart LDH at an increasing oxidative stress. (C) 2010 Elsevier B.V. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Polycation, Thermodynamic stability, Oxidation
in
International Journal of Biological Macromolecules
volume
47
issue
1
pages
15 - 20
publisher
Elsevier
external identifiers
  • wos:000278695000004
  • scopus:77953022650
ISSN
1879-0003
DOI
10.1016/j.ijbiomac.2010.04.003
language
English
LU publication?
yes
id
2358b773-da2e-421a-bec8-b340ba02f302 (old id 1631022)
date added to LUP
2010-07-21 12:25:09
date last changed
2018-07-01 03:00:12
@article{2358b773-da2e-421a-bec8-b340ba02f302,
  abstract     = {Protein stability assessment of seven model proteins in the presence of low molecular weight polyethyleneimine (PEI, MW 2000 Da) was performed. Thermodynamic stability, monitored by circular dichroism (CD) spectroscopy, showed that the polymer did not have a major effect on the melting temperature (T-m) of the basic proteins - muscle lactate dehydrogenase (LDH), ribonuclease A, lysozyme and cutinase, while for the acidic ones - human growth hormone, human serum albumin and heart lactate dehydrogenase - there was a shift in T-m towards lower temperatures. The secondary structures of the basic proteins were essentially the same, with none or a slight increase in the CD spectra, in presence of the polymer. In the case of the acidic proteins, the CD spectra were diminished mostly due to phase separation. Assuming a homogeneous distribution of the net charge on the protein surface a quantitative inverse relationship was established between surface charge density of the acidic proteins and the PEI2000 concentration required for maximum flocculation. Despite lowering the thermal stability of acidic proteins, PEI2000 was seen to protect heart LDH at an increasing oxidative stress. (C) 2010 Elsevier B.V. All rights reserved.},
  author       = {Mazzaferro, Laura and Breccia, Javier D. and Andersson, Maria and Hitzmann, Bernd and Hatti-Kaul, Rajni},
  issn         = {1879-0003},
  keyword      = {Polycation,Thermodynamic stability,Oxidation},
  language     = {eng},
  number       = {1},
  pages        = {15--20},
  publisher    = {Elsevier},
  series       = {International Journal of Biological Macromolecules},
  title        = {Polyethyleneimine-protein interactions and implications on protein stability},
  url          = {http://dx.doi.org/10.1016/j.ijbiomac.2010.04.003},
  volume       = {47},
  year         = {2010},
}