<i>CDApps</i>: integrated software for experimental planning and data processing at beamline B23, Diamond Light Source. Corrigendum

Hussain, Rohanah; Benning, Kristian; Myatt, Daniel; Jávorfí, Tamás; Longo, Edoardo; Rudd, Timothy R.; Pulford, Bill; Siligardi, Giuliano

doi:10.1107/s1600577515007602

Cited by 24 publications

(27 citation statements)

References 1 publication

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“…UV‐denaturation experiments were performed at 20°C recording 30 consecutive repeated scans in the far UV region using a bandwidth 1.8 nm. All spectra were subtracted of the SRCD spectrum of the corresponding tested compounds and elaborated using CDApps and OriginPro2018 softwares.…”

Section: Methodsmentioning

confidence: 99%

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Influence of small molecules on the photo‐stability of water soluble porcine lens proteins

et al. 2020

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The eye lens is a biconvex structure composed of lens fibres, cells that lack of blood and nerve supply and of any organelle, allowing for a high concentration of water soluble proteins that determine the lens transparency and refractive index. The lens water soluble protein pool in mammals is composed of α-, β-, and γ-crystallins, the latter being involved in calcium homeostasis and having structural importance, the first playing a crucial role in preventing protein aggregation and the consequent lens obfuscation, which leads to the clinical outcome of cataract. Among different factors, oxidative stress, free radicals, and reactive oxygen species (ROSs) generated by the exposure to UV light are widely recognized to cause cataract formation. Taking advantage of synchrotron radiation circular dichroism, fluorescence, and circular dichroism spectroscopies, in the present study we investigate the influence of different small molecules with the potential to either quench ROS generation or to stabilize protein conformation. Therefore, ascorbic acid, an excellent antioxidant agent already present in the eye aqueous humour, has been tested along with ceftriaxone, mannitol and trehalose, which osmolyte activity was demonstrated interfering with model proteins misfolding. Our results showed that ascorbic acid strongly inhibits the ROS production without, however, preserving the native protein structure, whereas mannitol had no effect on the ROS production but retained better the secondary structure of WS proteins. Collectively, the use of a mixture of ascorbic acid and mannitol could be used to better protect eye lens proteins from ROS damage preventing the cataract onset. K E Y W O R D Scataract, crystallins, fluorescence, small molecule stabilizers, synchrotron radiation circular dichroism

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Section: Methodsmentioning

confidence: 99%

“…The estimation of the secondary structure content was performed using the CONTINLL algorithm, implemented in the CDApps software …”

Section: Methodsmentioning

confidence: 99%

Influence of small molecules on the photo‐stability of water soluble porcine lens proteins

et al. 2020

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“…All the spectra were corrected by subtracting the background signal of the buffer. Secondary structure estimations from CD spectra was carried out using the software CD Apps 42 and applying CONTILLN algorithm with reference data SP 43 43 . The molar ellipticity ([Θ]) was calculated according to the equation described in 44 .…”

Section: Methodsmentioning

confidence: 99%

Structure dynamics of ApoA-I amyloidogenic variants in small HDL increase their ability to mediate cholesterol efflux

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Nilsson

Lindvall

et al. 2020

Preprint

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24Specific mutations in Apolipoprotein A-I (ApoA-I) of high-density lipoprotein (HDL) are 25 responsible for a late-onset systemic amyloidosis. Carriers do not exhibit increased 26 cardiovascular disease risk despite reduced levels of ApoA-I/ HDL-cholesterol. To explain 27 this paradox, we show that the HDL particle profile of L75P and L174S patients presents a 28 higher relative abundance of the 8.4 nm vs 9.6 nm particles, and that serum from patients, as 29 well as reconstituted 8.4 and 9.6 nm HDL particles (rHDL), possess increased capacity to 30 catalyze cholesterol efflux from macrophages. Synchrotron radiation circular dichroism and 31 hydrogen-deuterium exchange revealed that the variants in 8.4 nm rHDL have altered 32 secondary structure composition and display a more flexible binding to lipids compared to 33 their native counterpart. The reduced HDL-cholesterol levels of patients carrying ApoA-I 34 amyloidogenic variants are thus balanced by higher proportion of small, dense HDL particles 35 and better cholesterol efflux due to altered, region-specific protein structure dynamics. 36 37 Keywords 38 Apolipoprotein A-I, amyloidosis, high-density lipoprotein, cholesterol efflux, cardiovascular 39 disease 40 41 Abbreviations 42 ABCA1, ATP binding cassette A1; ABCG1, ATP binding cassette G1, ApoA-I, apolipoprotein 43 A-I; ApoB, apolipoprotein B; CD, circular dichroism; CVD, cardiovascular disease; FC, 44 unesterified free cholesterol; HDL, high-density lipoprotein; HDX, hydrogen-deuterium 45 exchange; LCAT, lecithin-cholesteryl acyl transferase; PBS, phosphate buffer saline; POPC, 46 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine; rHDL, reconstituted HDL; SRCD, 47 Synchrotron Radiation Circular Dichroism; TEV, tobacco etch virus; Tm, transition 48 temperature; WT, wild-type.49 3 Main 50 Amyloidoses are a broad group of diseases caused by protein instability and misfolding that 51 leads to pathological aggregation of proteins as amyloid deposits in tissues and organs 1 .52 These amyloid deposits are either localized, as in Alzheimer's and Parkinson's diseases, or 53 systemic, as is the case of transthyretin and light-chain amyloidoses. The different types of 54 amyloidoses commonly lead to severe and age-related damage of the tissues where 55 aggregation takes place. The understanding of the determinants leading to protein fibril 56 formation and amyloidosis development is thus key for finding ways to develop efficient 57 treatments for the affected individuals.58 Apolipoprotein A-I (ApoA-I), associated with hereditary systemic amyloidosis, has a key role 59 for the transportation of cholesterol and lipids in the circulation between peripheral tissues 60 and the liver 2 . Following its synthesis in the liver and intestines, ApoA-I mediates this 61 transportation by the formation of high-density lipoprotein (HDL) particles. These load 62 cholesterol and lipids from macrophages at the artery wall via a regulated efflux mechanism 63 catalyzed by the cellular ATP-binding cassette (ABC)A1 receptor. HDLs are then c...

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“…SRCD measurements were performed using a 10 cm path length cell, 3 mm aperture diameter and 800 µl capacity using Module B with a 1 nm increment, 1 s integration time, and 1.2 nm bandwidth at 23°C. 13,14 The results obtained were processed using the CDApps programme [13][14][15] and Origin software (OriginLab™).…”

Section: Synchrotron Radiation Circular Dichroism Spectroscopymentioning

confidence: 99%

Highly specific targeting of human acute myeloid leukaemia cells using pharmacologically active nanoconjugates

et al. 2018

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CDApps: integrated software for experimental planning and data processing at beamline B23, Diamond Light Source. Corrigendum

Cited by 24 publications

References 1 publication

Influence of small molecules on the photo‐stability of water soluble porcine lens proteins

Influence of small molecules on the photo‐stability of water soluble porcine lens proteins

Structure dynamics of ApoA-I amyloidogenic variants in small HDL increase their ability to mediate cholesterol efflux

Highly specific targeting of human acute myeloid leukaemia cells using pharmacologically active nanoconjugates

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