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240114s2024 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.3c02923
|2 doi
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|a pubmed25n1222.xml
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|a (DE-627)NLM366850318
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|a (NLM)38194428
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Yokoyama, Kazushige
|e verfasserin
|4 aut
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| 245 |
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|a Protein Corona Formation and Aggregation of Amyloid β 1-40-Coated Gold Nanocolloids
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|c 2024
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 24.01.2024
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|a Date Revised 15.02.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Amyloid fibrillogenesis is a pathogenic protein aggregation process that occurs through a highly ordered process of protein-protein interactions. To better understand the protein-protein interactions involved in amyloid fibril formation, we formed nanogold colloid aggregates by stepwise additions of ∼2 nmol of amyloid β 1-40 peptide (Aβ1-40) at pH ∼3.7 and ∼25 °C. The processes of protein corona formation and building of gold colloid [diameters (d) of 20 and 80 nm] aggregates were confirmed by a red-shift of the surface plasmon resonance (SPR) band, λpeak, as the number of Aβ1-40 peptides [N(Aβ1-40)] increased. The normalized red-shift of λpeak, Δλ, was correlated with the degree of protein aggregation, and this process was approximated as the adsorption isotherm explained by the Langmuir-Freundlich model. As the coverage fraction (θ) was analyzed as a function of ϕ, which is the N(Aβ1-40) per total surface area of nanogold colloids available for adsorption, the parameters for explaining the Langmuir-Freundlich model were in good agreement for both 20 and 80 nm gold, indicating that ϕ could define the stage of the aggregation process. Surface-enhanced Raman scattering (SERS) imaging was conducted at designated values of ϕ and suggested that a protein-gold surface interaction during the initial adsorption stage may be dependent on the nanosize. The 20 nm gold case seems to prefer a relatively smaller contacting section, such as a -C-N or C═C bond, but a plane of the benzene ring may play a significant role for 80 nm gold. Regardless of the size of the particles, the β-sheet and random coil conformations were considered to be used to form gold colloid aggregates. The methodology developed in this study allows for new insights into protein-protein interactions at distinct stages of aggregation
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Research Support, U.S. Gov't, Non-P.H.S.
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| 650 |
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|a Amyloid beta-Peptides
|2 NLM
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|a Gold
|2 NLM
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| 650 |
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|a 7440-57-5
|2 NLM
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| 650 |
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|a Protein Corona
|2 NLM
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| 650 |
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|a Protein Aggregates
|2 NLM
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| 650 |
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|a Gold Colloid
|2 NLM
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| 650 |
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|a Amyloid
|2 NLM
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| 650 |
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|a Peptide Fragments
|2 NLM
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| 700 |
1 |
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|a Barbour, Eli
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Hirschkind, Rachel
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Martinez Hernandez, Bryan
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Hausrath, Kaylee
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Lam, Theresa
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1985
|g 40(2024), 3 vom: 23. Jan., Seite 1728-1746
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnas
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| 773 |
1 |
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|g volume:40
|g year:2024
|g number:3
|g day:23
|g month:01
|g pages:1728-1746
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|u http://dx.doi.org/10.1021/acs.langmuir.3c02923
|3 Volltext
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