"RIV/00216224:14740/14:00073857" . . "7"^^ . . . . "136" . "Linse, S." . "V\u00E1cha, Robert" . "Lund, M." . . . . . . . "33" . . "Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides" . . "[31019671F66A]" . "US - Spojen\u00E9 st\u00E1ty americk\u00E9" . "http://pubs.acs.org/doi/abs/10.1021/ja505502e" . "BETA PROTEIN FIBRILLATION; ALPHA-SYNUCLEIN; POLYMERIC NANOPARTICLES; MEMBRANE INTERACTIONS; LIPID-BILAYERS; DRUG-DELIVERY; PHASE; NUCLEATION; INHIBITION; INTERFACES"@en . "0002-7863" . "Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides" . . "Journal of the American Chemical Society" . . . "P(ED1.1.00/02.0068), P(GA14-12598S)" . . "Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides"@en . . "Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides"@en . . "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." . "3"^^ . . . "14740" . "10.1021/ja505502e" . . "48631" . . "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 . . "RIV/00216224:14740/14:00073857!RIV15-MSM-14740___" . "1"^^ . "000340737900033" .