Determination of the Thickness of Interfacial Water by Time-Resolved Sum-Frequency Generation Vibrational Spectroscopy

Tan, Junjun; Wang, Mengmeng; Zhang, Jiahui; Ye, Shuji

doi:10.1021/acs.langmuir.3c02906

Cited by 7 publications

(2 citation statements)

References 85 publications

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“…The lifetime of amide A mode of β-sheet GP41 in D 2 O environment is 0.9 ps ( T nc ) while the lifetime of OH stretching at the DPPG bilayer/LKβ15 solution interface is approximately 0.10 ps ( T c ) (Figure S4). , The total lifetimes of the amide A mode from the lipid bilayer bound GP41 and LKβ15 at H 2 O interface were 0.73 (±0.05) and 0.56 (±0.05) ps, respectively, which yield an extent of water coupled to amide bond ( x %) of 21.3% and 42.5%. It is evident that the bandwidth of the amide I mode exhibits a strong linear correlation with the extent of amide bond coupled to water molecules (PWC extent) (Figure ).…”

Section: Resultsmentioning

confidence: 97%

Intermolecular Protein–Water Coupling Impedes the Coupling Between the Amide A and Amide I Mode in Interfacial Proteins

Tan,

Wang,

et al. 2024

Langmuir

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The coupling between different vibrational modes in proteins is essential for chemical dynamics and biological functions and is linked to the propagation of conformational changes and pathways of allosteric communication. However, little is known about the influence of intermolecular protein−H 2 O coupling on the vibrational coupling between amide A (NH) and amide I (C�O) bands. Here, we investigate the NH/CO coupling strength in various peptides with different secondary structures at the lipid cell membrane/H 2 O interface using femtosecond time-resolved sum frequency generation vibrational spectroscopy (SFG-VS) in which a femtosecond infrared pump is used to excite the amide A band, and SFG-VS is used to probe transient spectral evolution in the amide A and amide I bands. Our results reveal that the NH/CO coupling strength strongly depends on the bandwidth of the amide I mode and the coupling of proteins with water molecules. A large extent of protein−water coupling significantly reduces the delocalization of the amide I mode along the peptide chain and impedes the NH/CO coupling strength. A large NH/ CO coupling strength is found to show a strong correlation with the high energy transfer rate found in the light-harvesting proteins of green sulfur bacteria, which may understand the mechanism of energy transfer through a molecular system and assist in controlling vibrational energy transfer by engineering the molecular structures to achieve high energy transfer efficiency.

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Section: Resultsmentioning

confidence: 97%

Intermolecular Protein–Water Coupling Impedes the Coupling Between the Amide A and Amide I Mode in Interfacial Proteins

Tan,

Wang,

et al. 2024

Langmuir

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“…Herein, we propose a new method that uses the excitation percentage of molecular vibration in ultrafast interfacial vibrational dynamics to probe the near-field intensity of plasmonic substrates in MIR frequencies, which enables the detection of the electric field strength felt by the surface monolayer on substrates regardless of the surface molecular number. This method is based on a surface-sensitive femtosecond IR pump-sum frequency generation vibrational spectroscopy (SFG-VS) probe technique that has been demonstrated to be a powerful tool in determining interfacial structures and ultrafast dynamics. − It has been indicated that plasmon-enhanced nonlinear IR spectroscopies such as two-dimensional IR spectroscopy and IR pump–IR probe spectroscopy can also be used to estimate the local near-field enhancement by detecting the enhancement of nonlinear signals without knowledge of surface molecular coverage. − In comparison, SFG is a second-order nonlinear optical technique that allows the determination of molecular structure and dynamics at the surface and interface with submonolayer sensitivity and interface selectivity. ,, The IR pump-SFG probe method can detect the ultrafast vibrational dynamics of monolayers on metal surfaces.…”

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confidence: 99%

Probing the Local Near-Field Intensity of Plasmonic Nanoparticles in the Mid-infrared Spectral Region

Pei,

Zheng,

Tan

et al. 2024

J. Phys. Chem. Lett.

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The enhanced local field of gold nanoparticles (AuNPs) in mid-infrared spectral regions is essential for improving the detection sensitivity of vibrational spectroscopy and mediating photochemical reactions. However, it is still challenging to measure its intensity at subnanometer scales. Here, using the NO2 symmetric stretching mode (νNO2 ) of self-assembled 4-nitrothiophenol (4-NTP) monolayers on AuNPs as a model, we demonstrated that the percentage of excited νNO2 mode, determined by femtosecond time-resolved sum-frequency generation vibrational spectroscopy, allows us to directly detect the local field intensity of the AuNP surface in subnanometer ranges. The local-field intensity is tuned by AuNP diameters. An approximate 17-fold enhancement was observed for the local field on 80 nm AuNPs compared to the Au film. Additionally, the local field can regulate the anharmonicity of the νNO2 mode by synergistic effect with molecular orientation. This work offers a promising approach to probe the local field intensity distribution around plasmonic NP surfaces at subnanometer scales.

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Probing the Molecular Structure and Dynamics of Membrane‐Bound Proteins during Misfolding Processes by Sum‐Frequency Generation Vibrational Spectroscopy

Zheng,

Ni,

Pei

et al. 2024

ChemPlusChem

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Protein misfolding and amyloid formation are implicated in the protein dysfunction, but the underlying mechanism remains to be clarified due to the lack of effective tools for detecting the transient intermediates. Sum frequency generation vibrational spectroscopy (SFG‐VS) has emerged as a powerful tool for identifying the structure and dynamics of proteins at the interfaces. In this review, we summarize recent SFG‐VS studies on the structure and dynamics of membrane‐bound proteins during misfolding processes. This paper first introduces the methods for determining the secondary structure of interfacial proteins: combining chiral and achiral spectra of amide A and amide I bands and combining amide I, amide II, and amide III spectral features. To demonstrate the ability of SFG‐VS in investigating the interfacial protein misfolding and amyloid formation, studies on the interactions between different peptides/proteins (islet amyloid polypeptide, amyloid β, prion protein, fused in sarcoma protein, hen egg‐white lysozyme, fusing fusion peptide, class I hydrophobin SC3 and class II hydrophobin HFBI) and surfaces such as lipid membranes are discussed. These molecular‐level studies revealed that SFG‐VS can provide a unique understanding of the mechanism of interfacial protein misfolding and amyloid formation in real time, in situ and without any exogenous labeling.

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Determination of the Thickness of Interfacial Water by Time-Resolved Sum-Frequency Generation Vibrational Spectroscopy

Cited by 7 publications

References 85 publications

Intermolecular Protein–Water Coupling Impedes the Coupling Between the Amide A and Amide I Mode in Interfacial Proteins

Intermolecular Protein–Water Coupling Impedes the Coupling Between the Amide A and Amide I Mode in Interfacial Proteins

Probing the Local Near-Field Intensity of Plasmonic Nanoparticles in the Mid-infrared Spectral Region

Probing the Molecular Structure and Dynamics of Membrane‐Bound Proteins during Misfolding Processes by Sum‐Frequency Generation Vibrational Spectroscopy

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