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1. Functional dextran amino acid ester particles derived from N-protected S-trityl-L-cysteine.

Author

Bratuša A, Elschner T, Heinze T, Fröhlich E, Hribernik S, Božič M, Žagar E, Kleinschek KS, Thonhofer M, and Kargl R

Subjects
Cysteine chemistry, Dextrans chemistry, Particle Size, Surface Properties, Amino Acids chemistry, Cysteine analogs & derivatives, Esters chemistry
Abstract

This work describes the derivatization of dextran using N-(tert-butyloxycarbonyl)-S-(trityl)-L-cysteine in the presence of N,N'-carbonyldiimidazole (CDI) as a coupling agent. Homogeneous reactions in dimethyl sulfoxide allowed for an efficient coupling of the amino acid derivative to the polymer backbone. Derivatization was confirmed by infrared and 13 C NMR spectroscopy, size exclusion chromatography and elemental analysis. The presence of hydrophobic protecting groups resulted in a product that can be shaped into water-insoluble particles stable in an aqueous environment and non-toxic for lung epithelial cells. It is suggested that materials composed of ester bonds between amino acids and polysaccharides are useful for targeted drug delivery, bio-imaging or surface functionalization., (Copyright © 2019. Published by Elsevier B.V.)

Published
2019
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2. Facile fabrication and selective detection for cysteine of xylan/Au nanoparticles composite.

Author

Luo Y, Shen Z, Liu P, Zhao L, and Wang X

Subjects
Cysteine blood, Humans, Polysaccharides chemistry, Reducing Agents chemistry, Cysteine analysis, Gold chemistry, Limit of Detection, Metal Nanoparticles chemistry, Xylans chemistry
Abstract

This work reported a facile and green method to prepare highly stable and uniformly distributed Au nanoparticles (AuNPs), using biopolymer xylan as stabilizing and reducing agent. Full characterizations were performed and the results revealed that AuNPs were well dispersed with the diameters of 10-30nm. The optimal condition was as follows: the ratio of xylan to HAuCl4 was 150mg:15mg, reaction temperature was 80°C and reaction time was 40min. The xylan/AuNPs composite exhibited highly selective and sensitive sensing of cysteine in aqueous solution, it could distinguish cysteine among dozens kinds of amino acids, and the limit of detection (LOD) for cysteine was calculated as 0.57μM. Besides, the xylan/AuNPs composite was applied for Cys detection in human serum. This study provides a new way for high-value utilization of the rich biomass resource and a cheap, rapid and simple method for Cys detection in real biological samples., (Copyright © 2015 Elsevier Ltd. All rights reserved.)

Published
2016
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3. Mucin CYS domains are ancient and highly conserved modules that evolved in concert

Author

Jean-Luc Desseyn, Lille Inflammation Research International Center - U 995 (LIRIC), Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Institut de médecine predictive et de recherche thérapeutique (IMPRT), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Centre Régional de Lutte contre le Cancer Oscar Lambret [Lille] (UNICANCER/Lille), Université Lille Nord de France (COMUE)-UNICANCER-Université Lille Nord de France (COMUE)-UNICANCER-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille, Droit et Santé-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Université Lille 2 - Faculté de Médecine, The author gratefully acknowledges Dr. V. Gouyer (INSERM U795 and EA3925, Lille, France) and Pr. F. Gottrand (EA3925, University of Lille, France) for their critical comments. The author is indebted to Dr. P. Amieux (University of Washington, Seattle, WA) for help in improving the style of the paper., Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Université de Lille-UNICANCER-Université de Lille-UNICANCER-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille, Droit et Santé-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Faculté de Médecine Henri Warembourg - Université de Lille, and Lille Inflammation Research International Center - U 995 [LIRIC]

Subjects
MESH: Sequence Analysis, DNA, Animals, Conserved Sequence, Cysteine, Evolution, Molecular, Exons, Humans, Mucins, Phylogeny, Protein Interaction Domains and Motifs, Sequence Alignment, Sequence Analysis, DNA, [SDV]Life Sciences [q-bio], CYS domain, Genome, MUC5B, Exon, 0302 clinical medicine, Gel-forming mucin, MESH: Animals, MESH: Phylogeny, Genetics, 0303 health sciences, Concerted evolution, MESH: Conserved Sequence, Biochemistry, Coding repeats, MESH: Sequence Alignment, Biology, Evolution, Molecular, 03 medical and health sciences, MESH: Evolution, Molecular, MESH: Mucins/genetics, Amino acid residue, Molecular Biology, Gene, Ecology, Evolution, Behavior and Systematics, 030304 developmental biology, MESH: Protein Interaction Domains and Motifs, MESH: Humans, MESH: Mucins/metabolism, Mucin, Sequence Analysis, DNA, MUC5AC, MESH: Cysteine/genetics, Mucus, MUC2, MESH: Exons, 030217 neurology & neurosurgery, Function (biology)
Abstract

International audience; Background : Many large secreted gel-forming mucins contain multiple copies of a "naked" cysteine-enriched domain (CYS domain) that interrupt or are adjacent to mucin domains (Ser/Thr/Pro regions). There is less similarity of homologous CYS sequences between species than there is across CYS repeats within species. These CYS domains are likely implicated in reversible mucin-mucin interactions that play a central role in mucus properties. Results : The use of multiple genome sequences in a comparative analysis of CYS sequences identified new mucins containing the CYS domain in various species. Furthermore, analysis showed that this domain is at least 650 million-year old and that CYS sequences evolved under strong selective pressure in concerted fashion in all species examined by two mechanisms that never coexist within a given gene: either multiplication of exons encoding CYS modules or successive intra-exonic duplications. Conclusion : The CYS sequences appear to have undergone concerted evolution with a high selective pressure to conserve cysteine and other amino acid residues. This domain is the best-conserved domain in secreted mucins pointing toward an important common function in many different organisms.

Published
2008