Ni-S(uper)O(xide)D(ismutase) Inspired Ni(II)-Amino Acid Complexes Covalently Grafted onto Merrifield’s Resin - Synthesis, Structure and Catalytic Activity

Csendes, Zita; Kiss, Janos T.; Kutus, Bence; Sipos, Pal; Pálinkó, Istvan

doi:10.4028/www.scientific.net/MSF.730-732.1012

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HomeMaterials Science ForumAdvanced Materials Forum VINi-S(uper)O(xide)D(ismutase) Inspired Ni(II)-Amino...

Ni-S(uper)O(xide)D(ismutase) Inspired Ni(II)-Amino Acid Complexes Covalently Grafted onto Merrifield’s Resin - Synthesis, Structure and Catalytic Activity

Abstract:

In this work the syntheses of covalently grafted Ni(II)-complexes formed with various N- or C-protected amino acid ligands (L-histidine, L-tyrosine, L-cysteine and L-cystine) inspired by the active site of the Ni-SOD enzyme are presented. Merrifield’s resin was used as support to mimic the proteomic skeleton of the enzyme. Conditions of the syntheses were altered and the structural features of the substances obtained were studied by infrared spectroscopy. It was found that the preparation of covalently anchored Ni(II)−amino acid complexes was successful in all cases. In many cases the structures of the anchored complexes and the coordinating groups substantially varied upon changing the conditions of the syntheses. The obtained materials were studied by energy dispersive X-ray fluorescence coupled to scanning electron microscope (SEM−EDX). All the covalently anchored materials displayed superoxide dismutase (SOD) activity and some proved to be exceptionally efficient in the biochemical test reaction.

Info:

Periodical:

Materials Science Forum (Volumes 730-732)

Main Theme:

Advanced Materials Forum VI

Edited by:

Ana Maria Pires Pinto and António Sérgio Pouzada

Pages:

1012-1017

DOI:

https://doi.org/10.4028/www.scientific.net/MSF.730-732.1012

Citation:

Z. Csendes et al., "Ni-S(uper)O(xide)D(ismutase) Inspired Ni(II)-Amino Acid Complexes Covalently Grafted onto Merrifield’s Resin - Synthesis, Structure and Catalytic Activity", Materials Science Forum, Vols. 730-732, pp. 1012-1017, 2013

Online since:

November 2012

Authors:

Zita Csendes, Janos T. Kiss, Bence Kutus, Pal Sipos, Istvan Pálinkó

Keywords:

Covalent Anchoring, FT-IR Spectroscopy, Merrifield's Resin, Ni(II)-Amino Acid Complexes, Superoxide Dismutase (SOD) Activity

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Abstract: Two fractions, such as Fr1-3 and Fr2-2, were obtain after separating and purifing crude kiwifruit glycoprotein by using Sepharose Cl-6B gel column and DEAE Sepharose Cl-6B ion exchange column. In the UV and Infrared Spectroscopy of Fr1-3 and Fr2-2, the characteristic absorption peaks of sugar and protein were both found.The molecular weight of Fr1-3 is 30497，the molecular weight of Fr2-2 is 28567. Both of Fr1-3 and Fr2-2 have 17 amino acids, However, the amino acid content of them is different.

1730

Process Optimization and Composition Analysis of Antioxidant Enzymatic Hydrolysate from Squid By-Products by Papain

Authors: Bin Wang, Jia Hui Ma, You Le Qu, Xian Wang, Li Li

Abstract: In order to evaluate the high-value application of squid by-products yielded hydrolysate, the process of preparation and purification technology, chemical composition and in vitro antioxidant activity of the hydrolysate were investigated. The optimal conditions of papain hydrolysis were obtained by single-factor experiments and orthogonal test with the DPPH• scavenging ratio as index, amino acid composition was analysed by automatic amino acid analyzer, the hydrolysate was isolated with a Sephadex G-25 column. Based on single-factor experiments, the hydrolysate with the DPPH• scavenging ratio being 53.96 % was gained under the optimal condition of enzymolysis temperature of 45 °C, enzymolysis time of 3 h, total enzyme dose of 1.2 %, and the pH value of 7. The protein content of the hydrolysate reached up to 17.53 %, and the essential amino acids were accounted for 51.06 % of total amino acids. The largest content amino acid was glutamic acid, which accounted for 10.74 % of total amino acids. Compared with the amino acid profiles recommended by FAO/WHO, the quality of the protein hydrolysate was high, as it was rich in essential amino acids, including isoleucine, leucine, lysine, methionine and cystine, threonine, tryptophan, and valine, which covered 88 %-100 % of the FAO/WHO recommended. The hydrolysate was divided into three fractions (F1-F3) using a Sephadex G-25 column, the F1 possessed the highest antioxidation activity with the reducing power, •OH and DPPH• scavenging ratio being 0.236, 18.13 % and 63.85 % at the concentration of 5 mg/mL. Compared with the retention time of the reduced glutathione chromatomap, the relative molecular mass of F1 was higher than 307, F2 and F3 was lower than 307. The result revealed that the protein hydrolysate from squid by-products by papain had strongly antioxidant capacity in vitro and high nutrition, and this finding provided a new way of advanced exploitation of squid scrap resources.

198

The Synthesis Characterization and Application of Amino-Modified Polymethylhydrosiloxane Softener

Authors: Xin Zhao, Wen Ying Zhu

Abstract: Abstract. Amino-silicone Softener Was Synthesized by the Hydrosilylation Reaction, with Dimethylaminoethyl Acrylate, Polymethylhydrosiloxane as the Raw Materials, and Chlorioplatinic Acid as the Catalyst. the Copolymer Was Analyzed Using Ir Spectroscopy, then Emulsified it and Used in the Linen Fabric. the Results Showed that the Amino Group Can Be Introducted to Silicone Side Chains through Hydrosilylation that Dimethylaminoethyl Acrylate Grafted with Polymethylhydrogensiloxane, Obtained with the Softness of the Amino-modified Silicone Oil.

390

Synthesis and Spectroscopic Properties of Novel Chiral Amino Acid Tailed Porphyrins

Authors: Jun Xue, Ya Jun Wang, Ming Yi Rao, Guo Tian Luo

Abstract: A new L-amino acid tailed porphyrins and its Zinc(Ⅱ) complex were synthesized by L-amino acid and 5-(2-ethoylphenyl)-10, 15,20-triphenylporphyrin.FAB-MS, UV-vis, IR element analysis and chemical analysis were used to determine the structures of the porphyrin and zinc(Ⅱ) complex.

2398

Green Synthesis of AgNPs Coated Mesoporous Silica Nanoparticles Using Tyrosine as Reducing/Stabilising Agent

Authors: Waranya Ratirotjanakul, Tanapon Sioloetwong, Teeraporn Suteewong, Pramuan Tangboriboonrat

Abstract: A novel, simple and environmental friendly approach to fabricate silver nanoparticles (AgNPs) on mesoporous silica nanoparticles (MSNs) using tyrosine (Tyr) as biological reducing agent was developed. The functionalization of Tyr with MSNs (Tyr-MSNs) (150 nm in length) by the sol-gel process was confirmed by the characteristic peaks of amino, carboxyl and silanol groups appeared in FTIR spectrum and the change of the zeta potential from 0 mV at pH 2 to-60 mV at pH 12. Then, AgNPs were formed on the surface of Tyr-MSNs (Tyr-MSN@AgNPs) via only reducibility from phenolic group of Tyr and catalytic activity from base at room temperature. TEM images and UV-Visible absorption band at 420 nm supported the obtained AgNPs (18 nm at pH 11) were tightly bound to Tyr-MSNs even after centrifugation at high speed. These Tyr-MSN@AgNPs would be potentially used as drug carrier in biomedical applications.