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Polyethyleneimine-protein interactions and implications on protein stability.

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 PEI(2000) concentration required for maximum flocculation. Despite lowering the thermal stability of acidic proteins, PEI(2000) was seen to protect heart LDH at an increasing oxidative stress.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Mazzaferro L,Breccia JD,Andersson MM,Hitzmann B,Hatti-Kaul R

doi

10.1016/j.ijbiomac.2010.04.003

subject

Has Abstract

pub_date

2010-07-01 00:00:00

pages

15-20

issue

1

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(10)00121-2

journal_volume

47

pub_type

杂志文章

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