Design and synthesis of a new class of arginine analogues with an improved anion binding site in the side chain

2005 ◽  
pp. 772 ◽  
Author(s):  
Carsten Schmuck ◽  
Lars Geiger
Keyword(s):  
Binding Site ◽  
Anion Binding ◽  
Side Chain ◽  
Design And Synthesis ◽  
New Class

scholarly journals Programmable two-dimensional nanocrystals assembled from POSS-containing peptoids as efficient artificial light-harvesting systems

2021 ◽  
Vol 7 (20) ◽  
pp. eabg1448
Author(s):  
Mingming Wang ◽  
Yang Song ◽  
Shuai Zhang ◽  
Xin Zhang ◽  
Xiaoli Cai ◽  
...  
Keyword(s):  
Electron Scattering ◽  
Live Cell Imaging ◽  
Light Harvesting ◽  
Building Blocks ◽  
Side Chain ◽  
Two Dimensional ◽  
Design And Synthesis ◽  
New Class ◽  
Harvesting Systems ◽  
Oligomeric Silsesquioxane

Inspired by the formation of hierarchically structured natural biominerals (e.g., bone and tooth), various sequence-defined polymers have been synthesized and exploited for design and synthesis of functional hybrid materials. Here, we synthesized a series of organic-inorganic hybrid peptoids by using polyhedral oligomeric silsesquioxane (POSS) nanoclusters as side chains at a variety of backbone locations. We further demonstrated the use of these hybrid peptoids as sequence-defined building blocks to assemble a new class of programmable two-dimensional (2D) nanocrystals. They are highly stable and exhibit an enhanced mechanical property and electron scattering due to the incorporated POSS nanoclusters. By varying peptoid side-chain chemistry, we further demonstrated the precise displacement of a large variety of function groups within these 2D nanocrystals and developed a highly efficient aqueous light-harvesting system for live cell imaging. Because these 2D nanocrystals are biocompatible and highly programmable, we expect that they offer unique opportunities for applications.

Investigation of the Histamine H3 Receptor Binding Site. Design and Synthesis of Hybrid Agonists with a Lipophilic Side Chain

2010 ◽  
Vol 53 (17) ◽  
pp. 6445-6456 ◽  
Author(s):  
Makoto Ishikawa ◽  
Takashi Watanabe ◽  
Toshiaki Kudo ◽  
Fumikazu Yokoyama ◽  
Miki Yamauchi ◽  
...  
Keyword(s):  
Binding Site ◽  
Receptor Binding ◽  
Side Chain ◽  
Receptor Binding Site ◽  
Histamine H3 Receptor ◽  
Design And Synthesis ◽  
H3 Receptor ◽  
Site Design ◽  
Histamine H3

scholarly journals Bfd, a New Class of [2Fe-2S] Protein That Functions in Bacterial Iron Homeostasis, Requires a Structural Anion Binding Site

Biochemistry ◽  
2018 ◽  
Vol 57 (38) ◽  
pp. 5533-5543 ◽  
Author(s):  
Harshani Wijerathne ◽  
Huili Yao ◽  
Yan Wang ◽  
Scott Lovell ◽  
Kevin P. Battaile ◽  
...  
Keyword(s):  
Binding Site ◽  
Iron Homeostasis ◽  
Anion Binding ◽  
New Class

Evidence for Impaired Hepatic Vitamin K1 Metabolism in Patients Treated with N-Methyl-Thiotetrazole Cephalosporins

1984 ◽  
Vol 51 (03) ◽  
pp. 358-361 ◽  
Author(s):  
H Bechtold ◽  
K Andrassy ◽  
E Jähnchen ◽  
J Koderisch ◽  
H Koderisch ◽  
...  
Keyword(s):  
Protein C ◽  
Oral Intake ◽  
Bleeding Complications ◽  
Side Chain ◽  
Acute Administration ◽  
Vitamin K1 ◽  
New Class ◽  
Parenteral Alimentation ◽  
Hepatocellular Regeneration ◽  
Echis Carinatus

SummaryIn 8 patients on no oral intake and with parenteral alimentation, administration of cephalosporins with N-methyl-thiotetrazole side chain (moxalactam, cefamandole), was associated with prolongation of prothrombin time, appearance in the circulation of descarboxy-prothrombin (counter immunoelectrophoresis and echis carinatus assay) and diminution of protein C. Acute administration of 10 mg vitamin Ki was followed by the transient appearance of vitamin K1 2,3-epoxide, indicating an impaired hepatocellular regeneration of vitamin K1 from the epoxide. Impaired hepatic vitamin K1 metabolism, tentatively ascribed to the N-methyl-thiotetrazole group, is one (but possibly not the only) cause of bleeding complications and depression of vitamin K1dependent procoagulants in patients treated with the new class of cephalosporins.

Schistosomal Sulfotransferase Interaction with Oxamniquine Involves Hybrid Mechanism of Induced-fit and Conformational Selection

2020 ◽  
Vol 16 (4) ◽  
pp. 451-459 ◽  
Author(s):  
Fortunatus C. Ezebuo ◽  
Ikemefuna C. Uzochukwu
Keyword(s):  
Molecular Dynamics ◽  
Amino Acid ◽  
Binding Energy ◽  
Binding Site ◽  
Conformational Dynamics ◽  
Side Chain ◽  
Amino Acid Residues ◽  
Conformational Selection ◽  
Hybrid Mechanism ◽  
Dynamics Simulations

Background: Sulfotransferase family comprises key enzymes involved in drug metabolism. Oxamniquine is a pro-drug converted into its active form by schistosomal sulfotransferase. The conformational dynamics of side-chain amino acid residues at the binding site of schistosomal sulfotransferase towards activation of oxamniquine has not received attention. Objective: The study investigated the conformational dynamics of binding site residues in free and oxamniquine bound schistosomal sulfotransferase systems and their contribution to the mechanism of oxamniquine activation by schistosomal sulfotransferase using molecular dynamics simulations and binding energy calculations. Methods: Schistosomal sulfotransferase was obtained from Protein Data Bank and both the free and oxamniquine bound forms were subjected to molecular dynamics simulations using GROMACS-4.5.5 after modeling it’s missing amino acid residues with SWISS-MODEL. Amino acid residues at its binding site for oxamniquine was determined and used for Principal Component Analysis and calculations of side-chain dihedrals. In addition, binding energy of the oxamniquine bound system was calculated using g_MMPBSA. Results: The results showed that binding site amino acid residues in free and oxamniquine bound sulfotransferase sampled different conformational space involving several rotameric states. Importantly, Phe45, Ile145 and Leu241 generated newly induced conformations, whereas Phe41 exhibited shift in equilibrium of its conformational distribution. In addition, the result showed binding energy of -130.091 ± 8.800 KJ/mol and Phe45 contributed -9.8576 KJ/mol. Conclusion: The results showed that schistosomal sulfotransferase binds oxamniquine by relying on hybrid mechanism of induced fit and conformational selection models. The findings offer new insight into sulfotransferase engineering and design of new drugs that target sulfotransferase.

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