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240726s2024 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.4c01201
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|a eng
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|a Ma, Yong-Hao
|e verfasserin
|4 aut
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|a Disulfide-Driven Charge and Hydrophobicity Rearrangement of Remodeled Membrane Proteins toward Amyloid-Type Aggregation
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|c 2024
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|a Text
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|a ƒa Online-Ressource
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|a Date Completed 06.08.2024
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|a Date Revised 06.08.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a As a common pathological hallmark, protein aggregation into amyloids is a highly complicated phenomenon, attracting extensive research interest for elucidating its structural details and formation mechanisms. Membrane deposition and disulfide-driven protein misfolding play critical roles in amyloid-type aggregation, yet the underlying molecular process remains unclear. Here, we employed sum frequency generation (SFG) vibrational spectroscopy to comprehensively investigate the remodeling process of lysozyme, as the model protein, into amyloid-type aggregates at the cell membrane interface. It was discovered that disulfide reduction concurrently induced the transition of membrane-bound lysozyme from predominantly α-helical to antiparallel β-sheet structures, under a mode switch of membrane interaction from electrostatic to hydrophobic, and subsequent oligomeric aggregation. These findings shed light on the systematic understanding of dynamic molecular mechanisms underlying membrane-interactive amyloid oligomer formation
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|a Journal Article
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|a Muramidase
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|a Amyloid
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| 650 |
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|a Protein Aggregates
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|a Wang, Chu
|e verfasserin
|4 aut
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1 |
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|a Yang, Jingjing
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Li, Bolin
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| 700 |
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|a Han, Xiaofeng
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|a Lu, Xiaolin
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1985
|g 40(2024), 31 vom: 06. Aug., Seite 16145-16150
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|g volume:40
|g year:2024
|g number:31
|g day:06
|g month:08
|g pages:16145-16150
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|u http://dx.doi.org/10.1021/acs.langmuir.4c01201
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