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Inhibition of IAPP and IAPP((20-29)) Fibrillation by Polymeric Nanoparticles

Cabaleiro-Lago, C.; Lynch, I.; Dawson, K. A. and Linse, Sara LU (2010) In Langmuir 26(5). p.3453-3461
Abstract
The fibrillation process of the islet amyloid polypeptide (IAPP) and its fragment (IAPP((20-29))) was studied by means of Thioflavin T (ThT) fluorescence and transmission electron microscopy in the absence and presence of N-isopropylacrylamide:N-tert-butylacrylamide (NiPAM:BAM) copolymeric nanoparticles. The process was found to be strongly affected by the presence of the nanoparticles, which retard protein fibrillation its a function of the chemical surface properties of the nanoparticles. The NiPAM:BAM ratio was varied front 50:50 to 100:0, The nanoparticles with higher fraction of NiPAM imposed the strongest retardation of IAPP and IAPP((20-29)) fibrillation. These particles have the strongest hydrogen bonding capacity due to the less... (More)
The fibrillation process of the islet amyloid polypeptide (IAPP) and its fragment (IAPP((20-29))) was studied by means of Thioflavin T (ThT) fluorescence and transmission electron microscopy in the absence and presence of N-isopropylacrylamide:N-tert-butylacrylamide (NiPAM:BAM) copolymeric nanoparticles. The process was found to be strongly affected by the presence of the nanoparticles, which retard protein fibrillation its a function of the chemical surface properties of the nanoparticles. The NiPAM:BAM ratio was varied front 50:50 to 100:0, The nanoparticles with higher fraction of NiPAM imposed the strongest retardation of IAPP and IAPP((20-29)) fibrillation. These particles have the strongest hydrogen bonding capacity due to the less bulky N-isopropyl group and thus less steric hindrance of the hydrogen-bonding groups of the nanoparticle polymer backbone. Kinetic fibrillation data, as monitored by ThT fluorescence and supported by surface plasmon resonance experiments, suggest that the peptide is strongly absorbed onto the surface of the nanoparticles. This interaction reduces the concentration of peptide free in solution available to proceed to fibrillation which results in an increased lag time of fibrillation, observed its it delayed onset of ThT fluorescence increase, plus it reduction of the amount of fibrils formed its indicated by the equilibrium values at the end of the fibrillation reaction. For the fragment (IAPP((20-29))) the presence of nanoparticles changes the mechanism of association from monomers to fibrils, by interfering with early oligomeric species along the fibrillation pathway. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Langmuir
volume
26
issue
5
pages
3453 - 3461
publisher
The American Chemical Society
external identifiers
  • wos:000274636900071
  • scopus:77749320957
ISSN
0743-7463
DOI
10.1021/la902980d
language
English
LU publication?
yes
id
32621791-9598-4df1-836a-d8874b39d9b6 (old id 1568496)
date added to LUP
2010-03-23 09:25:10
date last changed
2018-05-29 11:14:49
@article{32621791-9598-4df1-836a-d8874b39d9b6,
  abstract     = {The fibrillation process of the islet amyloid polypeptide (IAPP) and its fragment (IAPP((20-29))) was studied by means of Thioflavin T (ThT) fluorescence and transmission electron microscopy in the absence and presence of N-isopropylacrylamide:N-tert-butylacrylamide (NiPAM:BAM) copolymeric nanoparticles. The process was found to be strongly affected by the presence of the nanoparticles, which retard protein fibrillation its a function of the chemical surface properties of the nanoparticles. The NiPAM:BAM ratio was varied front 50:50 to 100:0, The nanoparticles with higher fraction of NiPAM imposed the strongest retardation of IAPP and IAPP((20-29)) fibrillation. These particles have the strongest hydrogen bonding capacity due to the less bulky N-isopropyl group and thus less steric hindrance of the hydrogen-bonding groups of the nanoparticle polymer backbone. Kinetic fibrillation data, as monitored by ThT fluorescence and supported by surface plasmon resonance experiments, suggest that the peptide is strongly absorbed onto the surface of the nanoparticles. This interaction reduces the concentration of peptide free in solution available to proceed to fibrillation which results in an increased lag time of fibrillation, observed its it delayed onset of ThT fluorescence increase, plus it reduction of the amount of fibrils formed its indicated by the equilibrium values at the end of the fibrillation reaction. For the fragment (IAPP((20-29))) the presence of nanoparticles changes the mechanism of association from monomers to fibrils, by interfering with early oligomeric species along the fibrillation pathway.},
  author       = {Cabaleiro-Lago, C. and Lynch, I. and Dawson, K. A. and Linse, Sara},
  issn         = {0743-7463},
  language     = {eng},
  number       = {5},
  pages        = {3453--3461},
  publisher    = {The American Chemical Society},
  series       = {Langmuir},
  title        = {Inhibition of IAPP and IAPP((20-29)) Fibrillation by Polymeric Nanoparticles},
  url          = {http://dx.doi.org/10.1021/la902980d},
  volume       = {26},
  year         = {2010},
}