Chirality Organization of Aniline Oligomers through Hydrogen Bonds of Amino Acid Moieties

2010 ◽  
Vol 75 (22) ◽  
pp. 7909-7912 ◽  
Author(s):  
Satoshi D. Ohmura ◽  
Toshiyuki Moriuchi ◽  
Toshikazu Hirao
Keyword(s):  
Amino Acid ◽  
Hydrogen Bonds ◽  
Aniline Oligomers ◽  
Chirality Organization

scholarly journals DESIGN AND SYNTHESIS OF MOLECULAR TWEEZER BASED ON 3-HYDROXYFLAVONE FOR THE DETECTION OF ATP

2017 ◽  
pp. 67-70
Author(s):  
O. Bugera ◽  
A. Netrebchuk ◽  
V. Pivovarenko
Keyword(s):  
Amino Acid ◽  
Hydrogen Bonds ◽  
Atmospheric Oxygen ◽  
High Sensitivity ◽  
Fluorescence Probes ◽  
Amino Acid Derivative ◽  
One Pot ◽  
Design And Synthesis ◽  
Sensitivity And Selectivity ◽  
Molecular Tweezer

Adenosine 5'-triphosphate (ATP) is known as a universal energy source and signaling mediator in numerous biological processes. Among the methods for its determination, molecular fluorescence probes occupy leading positions due to high sensitivity and selectivity. Recently we have shown that 31 of 33 tested flavones and quinolones of various structures give fluorescence response and can be effectively applied as the probes in aqueous solutions for detection of ATP in 1–50,000 μM range of its concentrations. To increase response parameters of a probe in respect to ATP we have synthesized N,N'-(butane-1,4-diyl)bis(2-((2-(4-(dimethylamino)phenyl)-3-hydroxy-4-oxo-4H-chromene-6-yl)oxy)acetamide, the molecular tweezer composed of two flavonol units connected by active linker. On our idea, being equipped by two planar platforms, the tweezershould demonstrate increased affinity and selectivity to ATP in a result of increased number of hydrogen bonds and increased stacking interactions. Having two NH-amide groups the amino acid linker will form hydrogen bonds with the phosphates of ATP, increasing the portion of probe-ATP complex population in the reporting conformation.In the four-step synthesis of this molecular device, starting from methyl 2-(3-acetyl-4-hydroxyphenoxy)acetate and N,N-dimethylaminobenzaldehyde, the conditions for the reaction of one-pot chalcone formation and its oxidative heterocyclization in the presence of an organic base were found, which resulted in the isolation of a target flavonol-amino acid derivative with high yields. We suggest that atmospheric oxygen was an oxidizer in this process. The obtained derivative was converted intotarget compound by dual condensation with 1,4-butane diamine.

Strengths of Hydrogen Bonds Involving Phosphorylated Amino Acid Side Chains

2007 ◽  
Vol 129 (4) ◽  
pp. 820-827 ◽  
Author(s):  
Daniel J. Mandell ◽  
Ilya Chorny ◽  
Eli S. Groban ◽  
Sergio E. Wong ◽  
Elisheva Levine ◽  
...  
Keyword(s):  
Amino Acid ◽  
Hydrogen Bonds ◽  
Side Chains ◽  
Phosphorylated Amino Acid ◽  
Amino Acid Side Chains

scholarly journals The cyclol hypothesis and the “globular” proteins

1937 ◽  
Vol 161 (907) ◽  
pp. 505-524 ◽  
Keyword(s):  
Amino Acid ◽  
Hydrogen Bonds ◽  
Ad Hoc ◽  
Globular Proteins ◽  
The Body ◽  
Amino Acid Residues ◽  
Native Protein ◽  
Orderly Arrangement

A number of facts relating to proteins suggest that the polypeptides in native protein are in a folded state (Astbury 1933, 1934; Astbury and Street 1930, 1931; Pryde 1931; Wrinch 1936 a , b , c , 1937 a ; Langmuir, Schaefer and Wrinch 1937). The type of folding must be such as to imply the possibility of the regular and orderly arrangement of hundreds 01 amino-acid residues which to some extent at least is independent of the particular residues in question. We propose therefore to formulate all types of folding which are geometrically possible. Each hypothesis in turn can then be tested in two ways. We may consider its plausibility in itself: and having developed its implications to the farthest possible point, we may test it against known facts by ad hoc experiments. At present two types of folding have been suggested—by means of cyclol links (Wrinch 1936 a , b , c , 1937 a ; Langmuir, Schaefer and Wrinch 1937; Astbury 1936 a , b , c ; Frank, 1936) and by means of hydrogen bonds (Jordan Lloyd 1932; Jordan Lloyd and Marriott 1933; Mirsky and Pauling 1936; Wrinch and Jordan Lloyd 1936). The search for other types of folding is being continued. So far it has not proved possible to discard either theory on the grounds that the type of link postulated is out of the question. It is there­ fore very desirable to test these theories by means of their implications. Accordingly, on this occasion we consider (Wrinch 1937 b , c ) whether the cyclol theory can stand the test of the body of facts relating to the “globular” proteins, established by Svedberg and his collaborators (Svedberg and others 1929, 1930 a , b , 1934 a , b , 1935).

scholarly journals N-(β-Carboxyethyl)-α-isoleucine

2013 ◽  
Vol 69 (2) ◽  
pp. o172-o173 ◽  
Author(s):  
Irene Nehls ◽  
Olaf Hanebeck ◽  
Roland Becker ◽  
Franziska Emmerling
Keyword(s):  
Crystal Structure ◽  
Biological Activity ◽  
Amino Acid ◽  
Hydrogen Bonds ◽  
Title Compound ◽  
Addition Reaction ◽  
Three Dimensional ◽  
Dimensional Network

The title compound, {2-[(2-carbamoylethyl)amino]-3-methylpentanoic acid}, C9H18N2O3, is of interest with respect to its biological activity. It was formed during an addition reaction between acrylamide and the amino acid isoleucine. The crystal structure is a three-dimensional network built up by intermolecular N—H...O and O—H...N hydrogen bonds.

The conformational restriction of synthetic peptides, including a malaria peptide, for use as immunogens

1989 ◽  
Vol 323 (1217) ◽  
pp. 565-572 ◽  
Keyword(s):  
Hydrogen Bond ◽  
Plasmodium Falciparum ◽  
Amino Acid ◽  
Hydrogen Bonds ◽  
Synthetic Peptides ◽  
Synthetic Methods ◽  
Amide Hydrogen ◽  
Conformational Restriction ◽  
Conformationally Restricted ◽  
New Strategy

A new strategy is advanced for the conformational restriction of peptidyl immunogens. Our approach is to replace putative amide-amide hydrogen bonds with covalent hydrogen-bond mimics. Because on average every other amino acid in a protein engages in this bond, the syntheses of diversely shaped peptides can be contemplated. Synthetic methods for introducing a potential hydrogen-bond mimic into a peptide with α-helical potential is reported and the structural consequences are discussed. The replacement of the hydrogen bond with a chemical link will modify as well as shape the peptide. To explore the consequences of these changes, a potential synthetic vaccine for malaria, the repeating tetrapeptide Asn-Pro-Asn-Ala, was conformationally restricted. Antibodies to the shaped malarial peptide showed a strong cross reaction with Plasmodium falciparum sporozoites.

scholarly journals Probing the determinants of protein stability: comparison of class A β-lactamases

1995 ◽  
Vol 308 (3) ◽  
pp. 859-864 ◽  
Author(s):  
M Vanhove ◽  
S Houba ◽  
J Lamotte-Brasseur ◽  
J M Frère
Keyword(s):  
Amino Acid ◽  
Hydrogen Bonds ◽  
Bacterial Species ◽  
Three Dimensional ◽  
Peptide Bond ◽  
Minor Role ◽  
Salt Bridges ◽  
Beta Lactamases ◽  
Class A ◽  
Intramolecular Hydrogen

Five class A beta-lactamases produced by various mesophilic bacterial species have been compared. Although closely related in primary and overall structures, these enzymes exhibit very different stabilities. In order to investigate the factors responsible for these differences, several features deduced from the amino acid composition and three-dimensional structures were studied for the five proteins. This analysis revealed that higher stability appeared to correlate with increased numbers of intramolecular hydrogen bonds and of salt bridges. By contrast, the global hydrophobicity of the protein seemed to play a relatively minor role. A strongly unfavourable balance between charged residues and the presence of a cis-peptide bond preceding a non-proline residue might also contribute to the particularly low stability of two of the enzymes.

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