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

Chirality ◽  
2020 ◽  
Vol 32 (5) ◽  
pp. 611-618
Author(s):  
Claudia Honisch ◽  
Rohanah Hussain ◽  
Giuliano Siligardi ◽  
Paolo Ruzza
Keyword(s):  
Small Molecules ◽  
Water Soluble ◽  
Lens Proteins ◽  
Photo Stability ◽  
Stability Of Water

scholarly journals N-methyl mesoporphyrin IX as a highly selective light-up probe for G-quadruplex DNA

2019 ◽  
Vol 23 (11n12) ◽  
pp. 1195-1215 ◽  
Author(s):  
Ariana Yett ◽  
Linda Yingqi Lin ◽  
Dana Beseiso ◽  
Joanne Miao ◽  
Liliya A. Yatsunyk
Keyword(s):  
Optical Properties ◽  
Small Molecules ◽  
Genomic Stability ◽  
Water Soluble ◽  
Biological Processes ◽  
Binding Properties ◽  
Quadruplex Dna ◽  
Dna Structures ◽  
G Quadruplex ◽  
High Fluorescence

[Formula: see text]-methyl mesoporphyrin IX (NMM) is a water-soluble, non-symmetric porphyrin with excellent optical properties and unparalleled selectivity for G-quadruplex (GQ) DNA. G-quadruplexes are non-canonical DNA structures formed by guanine-rich sequences. They are implicated in genomic stability, longevity, and cancer. The ability of NMM to selectively recognize GQ structures makes it a valuable scaffold for designing novel GQ binders. In this review, we survey the literature describing the GQ-binding properties of NMM as well as its wide utility in chemistry and biology. We start with the discovery of the GQ-binding properties of NMM and the development of NMM-binding aptamers. We then discuss the optical properties of NMM, focusing on the light-switch effect — high fluorescence of NMM induced upon its binding to GQ DNA. Additionally, we examine the affinity and selectivity of NMM for GQs, as well as its ability to stabilize GQ structures and favor parallel GQ conformations. Furthermore, a portion of the review is dedicated to the applications of NMM-GQ complexes as biosensors for heavy metals, small molecules ([Formula: see text] ATP and pesticides), DNA, and proteins. Finally and importantly, we discuss the utility of NMM as a probe to investigate the roles of GQs in biological processes.

Water-soluble pH neutral triazatruxene-based small molecules as hole injection materials for solution-processable organic light-emitting diodes

2019 ◽  
Vol 7 (26) ◽  
pp. 7900-7905 ◽  
Author(s):  
Yonghong Chen ◽  
Xiaofu Wu ◽  
Yang Liu ◽  
Liang Chen ◽  
Hua Li ◽  
...  
Keyword(s):  
Small Molecules ◽  
Light Emitting Diodes ◽  
Water Soluble ◽  
Organic Light Emitting Diodes ◽  
Hole Injection ◽  
Light Emitting ◽  
Organic Light ◽  
Solution Processable ◽  
Injection Materials

Water-soluble and pH neutral triazatruxene-based small molecules have been used as hole injection materials in solution-processable organic light-emitting diodes, achieving even better performance compared with PEDOT:PSS.

Formation and Stability of Water-Soluble, Molecular Polyelectrolyte Complexes: Effects of Charge Density, Mixing Ratio, and Polyelectrolyte Concentration

Langmuir ◽  
2009 ◽  
Vol 25 (11) ◽  
pp. 6113-6121 ◽  
Author(s):  
Alexander Shovsky ◽  
Imre Varga ◽  
Ričardas Makuška ◽  
Per M. Claesson
Keyword(s):  
Charge Density ◽  
Water Soluble ◽  
Mixing Ratio ◽  
Polyelectrolyte Complexes ◽  
Stability Of Water

The stability of water-soluble modified starch iodophors

2013 ◽  
Vol 63 (1) ◽  
Author(s):  
V. Navikaitė ◽  
P. P. Danilovas ◽  
R. Klimavičiūtė ◽  
J. Bendoraitienė
Keyword(s):  
Water Soluble ◽  
Modified Starch ◽  
The Stability ◽  
Stability Of Water

scholarly journals Structure Elucidation of a Novel Yellow Chromophore from Human Lens Protein

2004 ◽  
Vol 279 (44) ◽  
pp. 45441-45449 ◽  
Author(s):  
Rongzhu Cheng ◽  
Qi Feng ◽  
Ognyan K. Argirov ◽  
Beryl J. Ortwerth
Keyword(s):  
Mass Spectrometry ◽  
Liquid Chromatography ◽  
Water Soluble ◽  
Human Lens ◽  
Lens Protein ◽  
Two Dimensional ◽  
Cross Link ◽  
Lens Proteins ◽  
Lysine Residues ◽  
Normal Human

We report here the isolation of a novel acid-labile yellow chromophore from the enzymatic digest of human lens proteins and the identification of its chemical structure by liquid chromatography-mass spectrometry, liquid chromatography-tandem mass spectrometry, and1H,13C, and two-dimensional NMR. This new chromophore exhibited a UV absorbance maximum at 343 nm and fluorescence at 410 nm when excited at 343 nm. Analysis of the purified compound by reversed-phase HPLC with in-line electrospray ionization mass spectrometry revealed a molecular mass of 370 Da. One- and two-dimensional NMR analyses elucidated the structure to be 1-(5-amino-5-carboxypentyl)-4-(5-amino-5-carboxypentylamino)-3-hydroxy-2,3-dihydropyridinium, a cross-link between the ϵ-amino groups of two lysine residues, and a five-carbon ring. Because this cross-link contains two lysine residues and a dihydropyridinium ring, we assigned it the trivial name of K2P. Quantitative determinations of K2P in individual normal human lens or cataract lens water-soluble and water-insoluble protein digests were made using a high-performance liquid chromatograph equipped with a diode array detector. These measurements revealed a significant enhancement of K2P in cataract lens proteins (613 ± 362 pmol/mg of water-insoluble sonicate supernatant (WISS) protein or 85 ± 51 pmol/mg of WS protein) when compared with aged normal human lens proteins (261 ± 93 pmol/mg of WISS protein or 23 ± 15 pmol/mg of water-soluble (WS) protein). These data provide chemical evidence for increased protein cross-linking during aging and cataract developmentin vivo. This new cross-link may serve as a quantitatively more significant biomarker for assessing the role of lens protein modifications during aging and in the pathogenesis of cataract.

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