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  1. Article ; Online: Using 2D-IR Spectroscopy to Measure the Structure, Dynamics, and Intermolecular Interactions of Proteins in H

    Hunt, Neil T

    Accounts of chemical research

    2024  Volume 57, Issue 5, Page(s) 685–692

    Abstract: ConspectusInfrared (IR) spectroscopy probes molecular structure at the level of the chemical bond or functional group. In the case of proteins, the most informative band in the IR spectrum is the amide I band, which arises predominantly from the C═O ... ...

    Abstract ConspectusInfrared (IR) spectroscopy probes molecular structure at the level of the chemical bond or functional group. In the case of proteins, the most informative band in the IR spectrum is the amide I band, which arises predominantly from the C═O stretching vibration of the peptide link. The folding of proteins into secondary and tertiary structures leads to vibrational coupling between peptide units, generating specific amide I spectral signatures that provide a fingerprint of the macromolecular conformation. Ultrafast two-dimensional IR (2D-IR) spectroscopy allows the amide I band of a protein to be spread over a second frequency dimension in a way that mirrors 2D-NMR methods. This means that amide I 2D-IR spectroscopy produces a spectral map that is exquisitely sensitive to protein structure and dynamics and so provides detailed insights that cannot be matched by IR absorption spectroscopy. As a result, 2D-IR spectroscopy has emerged as a powerful tool for probing protein structure and dynamics over a broad range of time and length scales in the solution phase at room temperature. However, the protein amide I band coincides with an IR absorption from the bending vibration of water (δ
    MeSH term(s) Spectrophotometry, Infrared/methods ; Proteins/chemistry ; Peptides ; Amides/chemistry ; Vibration ; Solvents
    Chemical Substances Proteins ; Peptides ; Amides ; Solvents
    Language English
    Publishing date 2024-02-16
    Publishing country United States
    Document type Review ; Journal Article
    ZDB-ID 1483291-4
    ISSN 1520-4898 ; 0001-4842
    ISSN (online) 1520-4898
    ISSN 0001-4842
    DOI 10.1021/acs.accounts.3c00682
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Biomolecular infrared spectroscopy: making time for dynamics.

    Hunt, Neil T

    Chemical science

    2023  Volume 15, Issue 2, Page(s) 414–430

    Abstract: Time resolved infrared spectroscopy of biological molecules has provided a wealth of information relating to structural dynamics, conformational changes, solvation and intermolecular interactions. Challenges still exist however arising from the wide ... ...

    Abstract Time resolved infrared spectroscopy of biological molecules has provided a wealth of information relating to structural dynamics, conformational changes, solvation and intermolecular interactions. Challenges still exist however arising from the wide range of timescales over which biological processes occur, stretching from picoseconds to minutes or hours. Experimental methods are often limited by vibrational lifetimes of probe groups, which are typically on the order of picoseconds, while measuring an evolving system continuously over some 18 orders of magnitude in time presents a raft of technological hurdles. In this Perspective, a series of recent advances which allow biological molecules and processes to be studied over an increasing range of timescales, while maintaining ultrafast time resolution, will be reviewed, showing that the potential for real-time observation of biomolecular function draws ever closer, while offering a new set of challenges to be overcome.
    Language English
    Publishing date 2023-11-28
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2559110-1
    ISSN 2041-6539 ; 2041-6520
    ISSN (online) 2041-6539
    ISSN 2041-6520
    DOI 10.1039/d3sc05223k
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: 2D-IR spectroscopy of proteins in H

    Rutherford, Samantha H / Baker, Matthew J / Hunt, Neil T

    The Journal of chemical physics

    2023  Volume 158, Issue 3, Page(s) 30901

    Abstract: The form of the amide I infrared absorption band provides a sensitive probe of the secondary structure and dynamics of proteins in the solution phase. However, the frequency coincidence of the amide I band with the bending vibrational mode of ... ...

    Abstract The form of the amide I infrared absorption band provides a sensitive probe of the secondary structure and dynamics of proteins in the solution phase. However, the frequency coincidence of the amide I band with the bending vibrational mode of H
    MeSH term(s) Spectrophotometry, Infrared/methods ; Proteins/chemistry ; Solvents/chemistry ; Amides/chemistry ; Water/chemistry
    Chemical Substances Proteins ; Solvents ; Amides ; Water (059QF0KO0R)
    Language English
    Publishing date 2023-01-21
    Publishing country United States
    Document type Journal Article
    ZDB-ID 3113-6
    ISSN 1089-7690 ; 0021-9606
    ISSN (online) 1089-7690
    ISSN 0021-9606
    DOI 10.1063/5.0129480
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  4. Article ; Online: Understanding the [NiFe] Hydrogenase Active Site Environment through Ultrafast Infrared and 2D-IR Spectroscopy of the Subsite Analogue K[CpFe(CO)(CN)

    Procacci, Barbara / Wrathall, Solomon L D / Farmer, Amy L / Shaw, Daniel J / Greetham, Gregory M / Parker, Anthony W / Rippers, Yvonne / Horch, Marius / Lynam, Jason M / Hunt, Neil T

    The journal of physical chemistry. B

    2024  Volume 128, Issue 6, Page(s) 1461–1472

    Abstract: The [CpFe(CO)(CN) ...

    Abstract The [CpFe(CO)(CN)
    Language English
    Publishing date 2024-02-01
    Publishing country United States
    Document type Journal Article
    ISSN 1520-5207
    ISSN (online) 1520-5207
    DOI 10.1021/acs.jpcb.3c07965
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Tuning of B

    Camacho, Ines S / Wall, Emma / Sazanovich, Igor V / Gozzard, Emma / Towrie, Mike / Hunt, Neil T / Hay, Sam / Jones, Alex R

    Chemical communications (Cambridge, England)

    2023  Volume 59, Issue 87, Page(s) 13014–13017

    Abstract: Time-resolved infrared spectroscopy reveals the flow of electron density through coenzyme ... ...

    Abstract Time-resolved infrared spectroscopy reveals the flow of electron density through coenzyme B
    MeSH term(s) Photochemistry ; Cobamides ; Bacteria
    Chemical Substances cobamamide (F0R1QK73KB) ; Cobamides
    Language English
    Publishing date 2023-10-31
    Publishing country England
    Document type Journal Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d3cc03900e
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Optical Screening and Classification of Drug Binding to Proteins in Human Blood Serum.

    Rutherford, Samantha H / Hutchison, Christopher D M / Greetham, Gregory M / Parker, Anthony W / Nordon, Alison / Baker, Matthew J / Hunt, Neil T

    Analytical chemistry

    2023  Volume 95, Issue 46, Page(s) 17037–17045

    Abstract: Protein-drug interactions in the human bloodstream are important factors in applications ranging from drug design, where protein binding influences efficacy and dose delivery, to biomedical diagnostics, where rapid, quantitative measurements could guide ... ...

    Abstract Protein-drug interactions in the human bloodstream are important factors in applications ranging from drug design, where protein binding influences efficacy and dose delivery, to biomedical diagnostics, where rapid, quantitative measurements could guide optimized treatment regimes. Current measurement approaches use multistep assays, which probe the protein-bound drug fraction indirectly and do not provide fundamental structural or dynamic information about the
    MeSH term(s) Humans ; Serum Albumin/chemistry ; Serum/metabolism ; Serum Albumin, Human/chemistry ; Protein Binding ; Spectrum Analysis ; Pharmaceutical Preparations ; Binding Sites
    Chemical Substances Serum Albumin ; Serum Albumin, Human (ZIF514RVZR) ; Pharmaceutical Preparations
    Language English
    Publishing date 2023-11-08
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/acs.analchem.3c03713
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Temperature-Induced Effects on the Structure of Gramicidin S.

    Pfukwa, Ngaatendwe B C / Rautenbach, Marina / Hunt, Neil T / Olaoye, Olufemi O / Kumar, Vikas / Parker, Anthony W / Minnes, Lucy / Neethling, Pieter H

    The journal of physical chemistry. B

    2023  Volume 127, Issue 17, Page(s) 3774–3786

    Abstract: We report on the structure of Gramicidin S (GS) in a model membrane mimetic environment represented by the amphipathic solvent 1-octanol using one-dimensional (1D) and two-dimensional (2D) IR spectroscopy. To explore potential structural changes of GS, ... ...

    Abstract We report on the structure of Gramicidin S (GS) in a model membrane mimetic environment represented by the amphipathic solvent 1-octanol using one-dimensional (1D) and two-dimensional (2D) IR spectroscopy. To explore potential structural changes of GS, we also performed a series of spectroscopic measurements at differing temperatures. By analyzing the amide I band and using 2D-IR spectral changes, results could be associated to the disruption of aggregates/oligomers, as well as structural and conformational changes happening in the concentrated solution of GS. The ability of 2D-IR to enable differentiation in melting transitions of oligomerized GS structures is attributed to the sensitivity of the technique to vibrational coupling. Two melting transition temperatures were identified; at
    MeSH term(s) Gramicidin/chemistry ; Temperature ; Molecular Dynamics Simulation ; Protein Conformation, beta-Strand ; Solvents
    Chemical Substances Gramicidin (1405-97-6) ; Solvents
    Language English
    Publishing date 2023-04-26
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1520-5207
    ISSN (online) 1520-5207
    DOI 10.1021/acs.jpcb.2c06115
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Metasurface-enhanced mid-infrared spectroscopy in the liquid phase.

    Kharratian, Soheila / Conteduca, Donato / Procacci, Barbara / Shaw, Daniel J / Hunt, Neil T / Krauss, Thomas F

    Chemical science

    2022  Volume 13, Issue 43, Page(s) 12858–12864

    Abstract: Vibrational spectroscopy is an important tool in chemical and biological analysis. A key issue when applying vibrational spectroscopy to dilute liquid samples is the inherently low sensitivity caused by short interaction lengths and small extinction ... ...

    Abstract Vibrational spectroscopy is an important tool in chemical and biological analysis. A key issue when applying vibrational spectroscopy to dilute liquid samples is the inherently low sensitivity caused by short interaction lengths and small extinction coefficients, combined with low target molecule concentrations. Here, we introduce a novel type of surface-enhanced infrared absorption spectroscopy based on the resonance of a dielectric metasurface. We demonstrate that the method is suitable for probing vibrational bands of dilute analytes with a range of spectral linewidths. We observe that the absorption signal is enhanced by 1-2 orders of magnitude and show that this enhancement leads to a lower limit of detection compared to attenuated total reflection (ATR). Overall, the technique provides an important addition to the spectroscopist's toolkit especially for probing dilute samples.
    Language English
    Publishing date 2022-10-21
    Publishing country England
    Document type Journal Article
    ZDB-ID 2559110-1
    ISSN 2041-6539 ; 2041-6520
    ISSN (online) 2041-6539
    ISSN 2041-6520
    DOI 10.1039/d2sc03927c
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Measuring proteins in H

    Rutherford, Samantha H / Greetham, Gregory M / Parker, Anthony W / Nordon, Alison / Baker, Matthew J / Hunt, Neil T

    The Journal of chemical physics

    2022  Volume 157, Issue 20, Page(s) 205102

    Abstract: The ability of two-dimensional infrared (2D-IR) spectroscopy to measure the amide I band of proteins in ... ...

    Abstract The ability of two-dimensional infrared (2D-IR) spectroscopy to measure the amide I band of proteins in H
    MeSH term(s) Pilot Projects ; Spectrophotometry, Infrared ; Solvents ; Amides ; Water
    Chemical Substances Solvents ; Amides ; Water (059QF0KO0R)
    Language English
    Publishing date 2022-12-01
    Publishing country United States
    Document type Journal Article
    ZDB-ID 3113-6
    ISSN 1089-7690 ; 0021-9606
    ISSN (online) 1089-7690
    ISSN 0021-9606
    DOI 10.1063/5.0127680
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  10. Article ; Online: A review of the evidence for Mohs micrographic surgery. Part 2: basal cell carcinoma.

    Brown, Alistair C / Brindley, Luke / Hunt, William T N / Earp, Eleanor M / Veitch, David / Mortimer, Neil J / Salmon, Paul J M / Wernham, Aaron

    Clinical and experimental dermatology

    2022  Volume 47, Issue 10, Page(s) 1794–1804

    Abstract: Mohs micrographic surgery (MMS) is considered the gold-standard treatment for basal cell carcinoma (BCC) particularly for sites with a high-risk of incomplete excision such as the central face, for tumours with an aggressive growth pattern and consequent ...

    Abstract Mohs micrographic surgery (MMS) is considered the gold-standard treatment for basal cell carcinoma (BCC) particularly for sites with a high-risk of incomplete excision such as the central face, for tumours with an aggressive growth pattern and consequent unpredictable subclinical extension and for recurrent tumours. However, the process is more time-consuming than for standard excision (SE), and the magnitude of benefit is uncertain. This article aims to provide a more complete picture of current evidence, including a review of cosmetic outcomes, tissue-sparing ability and cost-effectiveness of MMS. Although robust evidence is lacking, there is a large volume of observational data supporting a low recurrence rate after MMS. The risk of incomplete excision and higher recurrence rate of standard excision favours the use of MMS at high-risk sites. There is some low-certainty evidence that MMS results in a smaller defect size compared with SE, and that incomplete excision with SE results in larger defects. Larger defects may affect cosmetic outcome but there is no direct evidence that MMS improves cosmetic outcome compared with SE. There is conflicting evidence regarding the cost of MMS compared with SE, as some studies consider MMS less expensive than SE and others consider it more expensive, which may reflect the healthcare setting. A multicentre 10-year randomized controlled trial comparing MMS and SE in the treatment of high-risk BCC would be desirable, but is unlikely to be feasible or ethical. Collection of robust registry data capturing both MMS and SE outcomes would provide additional long-term outcomes.
    MeSH term(s) Carcinoma, Basal Cell/pathology ; Carcinoma, Basal Cell/surgery ; Facial Neoplasms/pathology ; Humans ; Mohs Surgery/methods ; Multicenter Studies as Topic ; Neoplasm Recurrence, Local ; Randomized Controlled Trials as Topic ; Skin Neoplasms/pathology ; Skin Neoplasms/surgery ; Treatment Outcome
    Language English
    Publishing date 2022-07-12
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 195504-4
    ISSN 1365-2230 ; 0307-6938
    ISSN (online) 1365-2230
    ISSN 0307-6938
    DOI 10.1111/ced.15266
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