Heme binding site in apomyoglobin may be effectively targeted with small molecules to control aggregation

Azami-Movahed, Mehrnaz; Shariatizi, Sajad; Sabbaghian, Marjan; Ghasemi, Ali; Ebrahim‐Habibi, Azadeh; Nemat‐Gorgani, Mohsen

doi:10.1016/j.biocel.2012.10.004

Cited by 13 publications

(11 citation statements)

References 77 publications

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“…1,2 Investigating and understanding the driving forces responsible for these assembly processes is therefore extremely important as this may provide information which enables the aggregation to be controlled 3,4 or prevented. [5][6][7] The interactions of small molecules with aggregates and assemblies is also an area of considerable interest, with applications ranging from hydrogen storage in metal organic frameworks 8 to the various assays used for monitoring the growth of amyloid fibrils.…”

Section: Introductionmentioning

confidence: 99%

NMR Investigations of the Interaction Between the Azo-Dye Sunset Yellow and Fluorophenol

Katz

Day

2013

J. Phys. Chem. B

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Copyright and reuse:Sussex Research Online is a digital repository of the research output of the University.Copyright and all moral rights to the version of the paper presented here belong to the individual author(s) and/or other copyright owners. To the extent reasonable and practicable, the material made available in SRO has been checked for eligibility before being made available.Copies of full text items generally can be reproduced, displayed or performed and given to third parties in any format or medium for personal research or study, educational, or not-for-profit purposes without prior permission or charge, provided that the authors, title and full bibliographic details are credited, a hyperlink and/or URL is given for the original metadata page and the content is not changed in any way. [Abstract word count: 134]

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Section: Introductionmentioning

confidence: 99%

NMR Investigations of the Interaction Between the Azo-Dye Sunset Yellow and Fluorophenol

Katz

Day

2013

J. Phys. Chem. B

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“…5). It should also be noted that peptide 9 formed flaky aggregates which may be due amorphous β-sheets assemblies that may form prior to fibril formation [56–58]. …”

Section: Resultsmentioning

confidence: 99%

Aromaticity and amyloid formation: Effect of π-electron distribution and aryl substituent geometry on the self-assembly of peptides derived from hIAPP22–29

Profit¹,

Vedad²,

SALEH³

et al. 2015

Archives of Biochemistry and Biophysics

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A comprehensive investigation of peptides derived from the 22–29 region of human islet amyloid polypeptide (hIAPP) that contain phenylalanine analogs at position 23 with a variety of electron donating and withdrawing groups, along with heteroaromatic surrogates, has been employed to interrogate how π-electron distribution effects amyloid formation. Kinetic aggregation studies using turbidity measurements indicate that electron rich aromatic ring systems consistently abolish the amyloidogenic propensity of hIAPP22–29. Electron poor systems modulate the rate of aggregation. Raman and Fourier transform infrared spectroscopy confirm the parallel β-sheet secondary structure of aggregates derived from peptides containing electron poor phenylalanine analogs and provide direct evidence of ring stacking. Transmission electron microscopy confirms the presence of amyloid fibrils. The effect of aryl substituent geometry on peptide self-assembly reveals that the electronic nature of substituents and not their steric profile is responsible for failure of the electron donating group peptides to aggregate. Non-aggregating hIAPP22–29 peptides were found to inhibit the self-assembly of full-length hIAPP1–37. The most potent inhibitory peptides contain phenylalanine with the p-amino and p-formamido functionalities. These novel peptides may serve as leads for the development of future aggregation inhibitors. A potential mechanism for inhibition of amylin self-assembly by electron rich hIAPP22–29 peptides is proposed.

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“…Protein–small molecule interaction has become a hot spot in the fields of biology, medicine, environmental science, and chemistry in recent decades . Using luminol as the CL probe, for example, the binding behaviors of bovine serum albumin with antibiotics and formaldehyde, lysozyme with lanthanide ions, and catalase with pesticides were reported by FI‐CL analysis.…”

Section: Introductionmentioning

confidence: 99%

Quantitative Monitoring of Rutin in Human Urine by Flow Injection-Chemiluminescence Analysis

Xin

et al. 2017

Journal of the Chinese Chemical Society

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In this paper, a rapid and sensitive flow injection‐chemiluminescence (FI‐CL) method is proposed for the quantitative determination of rutin based on the inhibitory effect of rutin on the chemiluminescence intensity from the luminol–chymotrypsin (CT) system. The decrease of CL intensity was found to be proportional to the logarithm of rutin concentration in the range 0.1–30.0 ng/mL. A method for the quantification of rutin is proposed, with the limit of detection (LOD) of 0.03 ng/mL (3σ). A complete analytical process including sampling and washing for rutin determination, which was conducted at a flow rate of 2.0 mL/min, could be performed completely within 30 s, yielding a sample efficiency of 120 h−1. The proposed procedure was successfully applied for the determination of rutin in human urine after oral intake, with recoveries varying from 93.9 to 108.1% and relative standard derivation <4.0% (n = 5). Results showed that urine reached the maximum concentration at ~2.5 h, and the total excretion ratios were (83.5 ± 0.6) and (86.8 ± 0.7)%, respectively, for two volunteers in 8 h. The pharmacokinetic parameters, including the half‐life (1.05 ± 0.02 h), absorption rate constant (1.18 ± 0.01 h−1), and elimination rate constant (0.70 ± 0.01 h−1), were obtained. The possible CL mechanism of the luminol–CT–rutin reaction is discussed by FI‐CL, fluorescence, and molecular docking methods.

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Heme binding site in apomyoglobin may be effectively targeted with small molecules to control aggregation

Cited by 13 publications

References 77 publications

NMR Investigations of the Interaction Between the Azo-Dye Sunset Yellow and Fluorophenol

NMR Investigations of the Interaction Between the Azo-Dye Sunset Yellow and Fluorophenol

Aromaticity and amyloid formation: Effect of π-electron distribution and aryl substituent geometry on the self-assembly of peptides derived from hIAPP22–29

Quantitative Monitoring of Rutin in Human Urine by Flow Injection-Chemiluminescence Analysis

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