Surface Effects on Aggregation Kinetics of Amyloidogenic
Peptides

J 2014

Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides

VÁCHA, Robert, S. LINSE a M. LUND

Základní údaje

Originální název

Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides

Autoři

VÁCHA, Robert (203 Česká republika, garant, domácí), S. LINSE (752 Švédsko) a M. LUND (752 Švédsko)

Vydání

Journal of the American Chemical Society, Washington, D.C. American Chemical Society, 2014, 0002-7863

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10403 Physical chemistry

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 12.113

Kód RIV

RIV/00216224:14740/14:00073857

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1021/ja505502e

UT WoS

000340737900033

Klíčová slova anglicky

BETA PROTEIN FIBRILLATION; ALPHA-SYNUCLEIN; POLYMERIC NANOPARTICLES; MEMBRANE INTERACTIONS; LIPID-BILAYERS; DRUG-DELIVERY; PHASE; NUCLEATION; INHIBITION; INTERFACES

Štítky

kontrola MP, podil, RIV, rivok, WOS

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 24. 10. 2014 10:46, Martina Prášilová

Anotace

V originále

The presence of surfaces influences the fibril formation kinetics of peptides and proteins. We present a systematic study of the aggregation kinetics of amyloidogenic peptides caused by different surfaces using molecular simulations of model peptides and thioflavin T fluorescence experiments. Increasing the monomer surface attraction affects the nucleation and growth of small oligomers in a nonlinear manner: Weakly attractive surfaces lead to retardation; strongly attractive surfaces lead to acceleration. Further, the same type of surface either accelerates or retards growth, depending on the bulk propensity of the peptide to form fibrils: An attractive surface retards fibril formation of peptides with a high tendency for fibril formation, while the same surface accelerates fibril formation of peptides with a low propensity for fibril formation. The surface effect is thus determined by the relative association propensity of peptides for the surface compared to bulk and by the surface area to protein concentration ratio. This rationalization is in agreement with the measured fibrillar growth of a-synuclein from Parkinson and amyloid beta peptide from Alzheimer disease in the presence of surface area introduced in a controlled way in the form of nanoparticles. These findings offer molecular insight into amyloid formation kinetics in complex environments and may be used to tune fibrillation properties in diverse systems.

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

GA14-12598S, projekt VaV

Název: Samouspořádané systémy amfifilních peptiů (Akronym: SAAP)

Investor: Grantová agentura ČR, Self-assembly of amphiphilic peptides with helical character

286154, interní kód MU

Název: SYLICA - Synergies of Life and Material Sciences to Create a New Future (Akronym: SYLICA)

Investor: Evropská unie, SYLICA - Synergies of Life and Material Sciences to Create a New Future, Kapacity

Citovat

VÁCHA, Robert, S. LINSE a M. LUND. Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides. Journal of the American Chemical Society. Washington, D.C.: American Chemical Society, 2014, roč. 136, č. 33, s. 11776-11782. ISSN 0002-7863. Dostupné z: https://dx.doi.org/10.1021/ja505502e.

@article{1197997,
   author = {Vácha, Robert and Linse, S. and Lund, M.},
   article_location = {Washington, D.C.},
   article_number = {33},
   doi = {http://dx.doi.org/10.1021/ja505502e},
   keywords = {BETA PROTEIN FIBRILLATION; ALPHA-SYNUCLEIN; POLYMERIC NANOPARTICLES; MEMBRANE INTERACTIONS; LIPID-BILAYERS; DRUG-DELIVERY; PHASE; NUCLEATION; INHIBITION; INTERFACES},
   language = {eng},
   issn = {0002-7863},
   journal = {Journal of the American Chemical Society},
   title = {Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides},
   url = {http://pubs.acs.org/doi/abs/10.1021/ja505502e},
   volume = {136},
   year = {2014}
}

TY  - JOUR
ID  - 1197997
AU  - Vácha, Robert - Linse, S. - Lund, M.
PY  - 2014
TI  - Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides
JF  - Journal of the American Chemical Society
VL  - 136
IS  - 33
SP  - 11776-11782
EP  - 11776-11782
PB  - American Chemical Society
SN  - 00027863
KW  - BETA PROTEIN FIBRILLATION
KW  - ALPHA-SYNUCLEIN
KW  - POLYMERIC NANOPARTICLES
KW  - MEMBRANE INTERACTIONS
KW  - LIPID-BILAYERS
KW  - DRUG-DELIVERY
KW  - PHASE
KW  - NUCLEATION
KW  - INHIBITION
KW  - INTERFACES
UR  - http://pubs.acs.org/doi/abs/10.1021/ja505502e
L2  - http://pubs.acs.org/doi/abs/10.1021/ja505502e
N2  - The presence of surfaces influences the fibril formation kinetics of peptides and proteins. We present a systematic study of the aggregation kinetics of amyloidogenic peptides caused by different surfaces using molecular simulations of model peptides and thioflavin T fluorescence experiments. Increasing the monomer surface attraction affects the nucleation and growth of small oligomers in a nonlinear manner: Weakly attractive surfaces lead to retardation; strongly attractive surfaces lead to acceleration. Further, the same type of surface either accelerates or retards growth, depending on the bulk propensity of the peptide to form fibrils: An attractive surface retards fibril formation of peptides with a high tendency for fibril formation, while the same surface accelerates fibril formation of peptides with a low propensity for fibril formation. The surface effect is thus determined by the relative association propensity of peptides for the surface compared to bulk and by the surface area to protein concentration ratio. This rationalization is in agreement with the measured fibrillar growth of a-synuclein from Parkinson and amyloid beta peptide from Alzheimer disease in the presence of surface area introduced in a controlled way in the form of nanoparticles. These findings offer molecular insight into amyloid formation kinetics in complex environments and may be used to tune fibrillation properties in diverse systems.
ER  -

VÁCHA, Robert, S. LINSE a M. LUND. Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides. \textit{Journal of the American Chemical Society}. Washington, D.C.: American Chemical Society, 2014, roč.~136, č.~33, s.~11776-11782. ISSN~0002-7863. Dostupné z: https://dx.doi.org/10.1021/ja505502e.

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