scholarly journals π–π Stacking assisted binding of aromatic amino acids by copper(ii)–aromatic diimine complexes. Effects of ring substituents on ternary complex stability

2007 ◽  
pp. 299-307 ◽  
Author(s):  
Tatsuo Yajima ◽  
Reiko Takamido ◽  
Yuichi Shimazaki ◽  
Akira Odani ◽  
Yasuo Nakabayashi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Ternary Complex ◽  
Aromatic Amino Acids ◽  
Complex Stability ◽  
Π Stacking ◽  
Diimine Complexes

Combined DFT and MD simulation studies of protein stability on imidazolium–water (ImH+Wn) clusters with aromatic amino acids

2020 ◽  
Vol 44 (41) ◽  
pp. 17912-17923
Author(s):  
Kandhan Palanisamy ◽  
Muthuramalingam Prakash ◽  
Varatharaj Rajapandian
Keyword(s):  
Amino Acids ◽  
Protein Stability ◽  
Md Simulation ◽  
Protein Denaturation ◽  
Aromatic Amino Acids ◽  
Simulation Studies ◽  
Π Stacking ◽  
Hydrated Clusters

The hydrated clusters of protonated imidazole (ImH+) can induce protein denaturation through various kinds of monovalent interactions such as cation···π (stacking), N–H⋯π (T-shaped) and water-mediated O–H⋯O H-bonds.

The Efficient Preparation of Radiolabeled Aromatic Amino Acids via Cu-Mediated Radiofluorination using Ni-complexes

2019 ◽  
Author(s):  
A Craig ◽  
N Kolks ◽  
E Urusova ◽  
BD Zlatopolskiy ◽  
B Neumaier
Keyword(s):  
Amino Acids ◽  
Aromatic Amino Acids

Long term dietary intake of aromatic amino acids are associated with leptin gene expression in adipose tissues of non-diabetic adults

2018 ◽  
Author(s):  
Golaleh Asghari ◽  
Emad Yuzbashian ◽  
Maryam Zarkesh ◽  
Parvin Mirmiran ◽  
Mehdi Hedayati ◽  
...  
Keyword(s):  
Gene Expression ◽  
Amino Acids ◽  
Dietary Intake ◽  
Aromatic Amino Acids ◽  
Adipose Tissues

Single Amino Acid Based Self-Assemblies of Cysteine and Methionine

2018 ◽  
Author(s):  
Nidhi Gour ◽  
Bharti Koshti ◽  
Chandra Kanth P. ◽  
Dhruvi Shah ◽  
Vivek Shinh Kshatriya ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Self Assembly ◽  
Aromatic Amino Acids ◽  
Neutral Condition ◽  
Single Amino Acid ◽  
Binding Assays ◽  
Human Neuroblastoma ◽  
Cytotoxicity Assays ◽  
First Time

We report for the very first time self-assembly of Cysteine and Methionine to discrenible strucutres under neutral condition. To get insights into the structure formation, thioflavin T and Congo red binding assays were done which revealed that aggregates may not have amyloid like characteristics. The nature of interactions which lead to such self-assemblies was purported by coincubating assemblies in urea and mercaptoethanol. Further interaction of aggregates with short amyloidogenic dipeptide diphenylalanine (FF) was assessed. While cysteine aggregates completely disrupted FF fibres, methionine albeit triggered fibrillation. The cytotoxicity assays of cysteine and methionine structures were performed on Human Neuroblastoma IMR-32 cells which suggested that aggregates are not cytotoxic in nature and thus, may not have amyloid like etiology. The results presented in the manuscript are striking, since to the best of our knowledge,this is the first report which demonstrates that even non-aromatic amino acids (cysteine and methionine) can undergo spontaneous self-assembly to form ordered aggregates.

Equilibrium Studies of Binary and Ternary Complexes of Palladium(II) Involving Amino Acids

1993 ◽  
Vol 58 (5) ◽  
pp. 1103-1108 ◽  
Author(s):  
Mohamed M. Shoukry ◽  
Eman M. Shoukry
Keyword(s):  
Amino Acids ◽  
Relative Stability ◽  
Ternary Complex ◽  
Formation Constants ◽  
Ternary Complexes ◽  
Conductivity Measurements ◽  
Equilibrium Studies ◽  
Binary And Ternary Complexes ◽  
Binary Complexes

The formation constants of the binary and ternary complexes of palladium(II) with diethylenetriamine and amino acids as ligands have been determined potentiometrically at 25 °C in 0.1 M NaNO3 solution. The relative stability of each ternary complex was compared with that of the corresponding binary complexes in terms of ∆logK values. The mode of chelation was ascertained by conductivity measurements.

Atypical amino acids inhibit histidine, valine, or lysine transport into rat brain

1983 ◽  
Vol 245 (4) ◽  
pp. R556-R563 ◽  
Author(s):  
J. K. Tews ◽  
A. E. Harper
Keyword(s):  
Amino Acids ◽  
Rat Brain ◽  
Blood Brain Barrier ◽  
Brain Slices ◽  
Aromatic Amino Acids ◽  
Brain Barrier ◽  
Basic Amino Acids ◽  
Large Neutral Amino Acids ◽  
Neutral Amino Acids ◽  
Single Meal

Transport of histidine, valine, or lysine into rat brain slices and across the blood-brain barrier (BBB) was determined in the presence of atypical nonprotein amino acids. Competitors of histidine and valine transport in slices were large neutral amino acids including norleucine, norvaline, alpha-aminooctanoate, beta-methylphenylalanine, and alpha-aminophenylacetate. Less effective were aromatic amino acids with ring substituents; ineffective were basic amino acids and omega-amino isomers of norleucine and aminooctanoate. Lysine transport was moderately depressed by homoarginine or ornithine plus arginine; large neutral amino acids were also similarly inhibitory. Histidine or valine transport across the BBB was also strongly inhibited by large neutral amino acids that were the most effective competitors in the slices (norvaline, norleucine, alpha-aminooctanoate, and alpha-aminophenylacetate); homoarginine and 8-aminooctanoate were ineffective. Homoarginine, ornithine, and arginine almost completely blocked lysine transport, but the large neutral amino acids were barely inhibitory. When rats were fed a single meal containing individual atypical large neutral amino acids or homoarginine, brain pools of certain large neutral amino acids or of arginine and lysine, respectively, were depleted.

Sign in / Sign up

Export Citation Format

Share Document