Inhibition of IAPP and IAPP((20-29)) Fibrillation by Polymeric Nanoparticles
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1568496
- author
- Cabaleiro-Lago, C. ; Lynch, I. ; Dawson, K. A. and Linse, Sara LU
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Langmuir
- volume
- 26
- issue
- 5
- pages
- 3453 - 3461
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000274636900071
- scopus:77749320957
- pmid:20017535
- 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
- 2016-04-01 10:07:07
- date last changed
- 2023-11-09 12:19:06
@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 (ACS)}},
series = {{Langmuir}},
title = {{Inhibition of IAPP and IAPP((20-29)) Fibrillation by Polymeric Nanoparticles}},
url = {{http://dx.doi.org/10.1021/la902980d}},
doi = {{10.1021/la902980d}},
volume = {{26}},
year = {{2010}},
}