About: Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides

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An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://pubs.acs.org/doi/abs/10.1021/ja505502e
Description	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 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. (en)
Title	Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides (en)
skos:prefLabel	Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides (en)
skos:notation	RIV/00216224:14740/14:00073857!RIV15-MSM-14740___
http://linked.open...avai/riv/aktivita	P
http://linked.open...avai/riv/aktivity	P(ED1.1.00/02.0068), P(GA14-12598S)
http://linked.open...iv/cisloPeriodika	33
http://linked.open...vai/riv/dodaniDat	2015
http://linked.open...aciTvurceVysledku	Vácha, Robert
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Masarykova univerzita / Středoevropský technologický institut
http://linked.open...dnocenehoVysledku	48631
http://linked.open...ai/riv/idVysledku	RIV/00216224:14740/14:00073857
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	BETA PROTEIN FIBRILLATION; ALPHA-SYNUCLEIN; POLYMERIC NANOPARTICLES; MEMBRANE INTERACTIONS; LIPID-BILAYERS; DRUG-DELIVERY; PHASE; NUCLEATION; INHIBITION; INTERFACES (en)
http://linked.open.../riv/klicoveSlovo	LIPID-BILAYERS INTERFACES ALPHA-SYNUCLEIN INHIBITION DRUG-DELIVERY PHASE BETA PROTEIN FIBRILLATION MEMBRANE INTERACTIONS NUCLEATION POLYMERIC NANOPARTICLES
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[31019671F66A]
http://linked.open...i/riv/nazevZdroje	Journal of the American Chemical Society
http://linked.open...in/vavai/riv/obor	CF
http://linked.open...ichTvurcuVysledku	1 (xsd:int)
http://linked.open...cetTvurcuVysledku	3 (xsd:int)
http://linked.open...vavai/riv/projekt	Central european institute of technology Samouspořádané systémy amfifilních peptiů
http://linked.open...UplatneniVysledku	2014
http://linked.open...v/svazekPeriodika	136
http://linked.open...iv/tvurceVysledku	Lund, M. Vácha, Robert Linse, S.
http://linked.open...ain/vavai/riv/wos	000340737900033
issn	0002-7863
number of pages	7 (xsd:int)
http://bibframe.org/vocab/doi	10.1021/ja505502e
http://localhost/t...ganizacniJednotka	14740

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