Low-Temperature Raman Spectra of l-Histidine Crystals

Sousa, G.P. De; Freire, Paulo; Filho, J. Mendes; Melo, F. E. A.; Luz-Lima, C.

doi:10.1007/s13538-013-0132-3

Cited by 13 publications

(6 citation statements)

References 30 publications

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“…An additional peak at 1612 cm –1 can also be assigned to the contribution of these three amino acid residues . Other vibration modes were observed at 1091 cm –1 (CN symmetric stretching), 1175 cm –1 (CH bending in-plane), 1275 cm –1 (amide III), 1449 cm –1 (CH bending), 1714 cm –1 (CO stretching), 2930 cm –1 (aliphatic CH stretching), and 3070 cm –1 (aromatic CH stretching). ,,, High intense peaks at 440 and 611 cm –1 for ADAM17cyto indicate the presence of SS and CS stretching, respectively. , The SS stretching mode might have two contributions, the first from the disulfide bond formed in the heterodimer between Trx-1 and ADAM17cyto and another related to the disulfide bond present in the ADAM17cyto structure. Although disulfide bond formation is a slow process at physiological pH (7.4), many proteins like ADAM17cyto and Trx-1 can interact through cysteine dimerization.…”

Section: Resultsmentioning

confidence: 96%

“…87,88,90,91 High intense peaks at 440 and 611 cm −1 for ADAM17cyto indicate the presence of SS and CS stretching, respectively. 87,92 The SS stretching mode might have two contributions, the first from the disulfide bond formed in the heterodimer between Trx-1 and ADAM17cyto and another related to the disulfide bond present in the ADAM17cyto structure. Although disulfide bond formation is a slow process at physiological pH (7.4), many proteins like ADAM17cyto and Trx-1 can interact through cysteine dimerization.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

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ZIF-8 Metal–Organic Framework Electrochemical Biosensor for the Detection of Protein–Protein Interaction

et al. 2021

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In this study, a novel label-free electrochemical biosensor based on the zeolitic imidazole framework (ZIF-8) was developed for monitoring protein–protein interactions (PPIs). ZIF-8 was deposited on interdigitated electrodes and employed as a transducing material and simultaneously carried the thioredoxin-1 (Trx-1) protein, followed by the deposition of increased concentrations of the cytoplasmic domain of a disintegrin and metalloproteinase 17 (ADAM17cyto) known as the Trx-1 binding partner. Structural and morphological characterizations were used to validate and verify the formation of ZIF-8. The ZIF-8 crystals showed a rhombic dodecahedral structure with mainly exposed (011) facets, a mean particle size of 205 (±22) nm, and a ZIF-8 film thickness around 61 (±6) nm. The interaction between Trx-1 and ADAM17cyto proteins was analyzed through electrochemical impedance spectroscopy (EIS). The results indicate a linear and inverse relationship between the impedance responses at 0.1 Hz for ADAM17cyto concentrations from 50 nM to 8 μM, with a coefficient of variation from 1.0% to 11.4%. The proposed biosensor also displayed a significant selectivity and stability verified by using ADAM17cyto mutant and BSA as controls. As a proof-of-concept, we compared the results with a widely used type of PPI assay based on antibody recognition, the solid-phase binding assay, using the same proteins. The solid-phase binding assay was able to detect a significant binding only in ADAM17cyto concentrations above 0.5 μM, with a coefficient of variation varying from 5.4% to 27.5%. The results demonstrate that the developed biosensor was 10× more sensitive and reproducible than the conventional solid-phase binding assay. Furthermore, the developed electrochemical biosensor based on ZIF-8 provides a faster, label-free, and low-cost detection analysis, representing a novel strategy in detecting PPIs.

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Section: Resultsmentioning

confidence: 96%

Section: ■ Results and Discussionmentioning

confidence: 99%

ZIF-8 Metal–Organic Framework Electrochemical Biosensor for the Detection of Protein–Protein Interaction

et al. 2021

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“…4c). The vibrational bands of the INS data of MOF-808 and MOF-808@His samples were identified on the basis of the bibliographic data based on the combination of experimental and computational studies (de Sousa et al 74 and Freire et al 75 ), as well as taking into account our preliminary studies in the MOF-808@Cys system. For instance, the assignation of the Raman and IR bands found in literature have been summarized in the Fig.…”

Section: Resultsmentioning

confidence: 99%

Enzyme-mimicking of copper-sites in metal–organic frameworks for oxidative degradation of phenolic compounds

Valverde,

Alkain,

Rio-López

et al. 2024

J. Mater. Chem. A

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“…Prior differential scanning calorimetry (DSC) analysis of powder samples performed by Supriya et al (2018) show the absence of a phase transition in the two polymorphs between $313 and 573 K. Other studies have revealed discontinuities in the Raman spectra of the orthorhombic form at 165 K and an enthalpic anomaly at around 160 K, also by DSC (De Sousa et al, 2013), suggesting a conformational phase transition. Further and more detailed temperature-dependent diffraction work around 165 K is needed to understand fully the phase behaviour of the orthorhombic form of l-histidine.…”

Section: Neutron Structures Of the Polymorphs At 295 K And The Effect Of Temperaturementioning

confidence: 99%

Accurate H-atom parameters for the two polymorphs of L-histidine at 5, 105 and 295 K

Novelli¹,

McMonagle²,

Kleemiss³

et al. 2021

Acta Crystallogr Sect B

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The crystal structure of the monoclinic polymorph of the primary amino acid L-histidine has been determined for the first time by single-crystal neutron diffraction, while that of the orthorhombic polymorph has been reinvestigated with an untwinned crystal, improving the experimental precision and accuracy. For each polymorph, neutron diffraction data were collected at 5, 105 and 295 K. Single-crystal X-ray diffraction experiments were also performed at the same temperatures. The two polymorphs, whose crystal packing is interpreted by intermolecular interaction energies calculated using the Pixel method, show differences in the energy and geometry of the hydrogen bond formed along the c direction. Taking advantage of the X-ray diffraction data collected at 5 K, the precision and accuracy of the new Hirshfeld atom refinement method implemented in NoSpherA2 were probed choosing various settings of the functionals and basis sets, together with the use of explicit clusters of molecules and enhanced rigid-body restraints for H atoms. Equivalent atomic coordinates and anisotropic displacement parameters were compared and found to agree well with those obtained from the corresponding neutron structural models.

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Low-Temperature Raman Spectra of l-Histidine Crystals

Cited by 13 publications

References 30 publications

ZIF-8 Metal–Organic Framework Electrochemical Biosensor for the Detection of Protein–Protein Interaction

ZIF-8 Metal–Organic Framework Electrochemical Biosensor for the Detection of Protein–Protein Interaction

Enzyme-mimicking of copper-sites in metal–organic frameworks for oxidative degradation of phenolic compounds

Accurate H-atom parameters for the two polymorphs of L-histidine at 5, 105 and 295 K

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