Conversion of l ‐Tryptophan Derivatives into Biologically Active Amino Acid Ionic Liquids

2021 ◽  
Vol 6 (22) ◽  
pp. 5614-5621
Author(s):  
Daria Szymaniak ◽  
Tomasz Kleiber ◽  
Marta Wojcieszak ◽  
Katarzyna Materna ◽  
Juliusz Pernak
Keyword(s):  
Ionic Liquids ◽  
Amino Acid ◽  
Biologically Active ◽  
Active Amino Acid ◽  
Tryptophan Derivatives

Stability Constants of Some Metal Complexes Formed by Mimosine and Related Compounds

1979 ◽  
Vol 32 (1) ◽  
pp. 21 ◽  
Author(s):  
H Stunzi ◽  
DD Perrin ◽  
T Teitei ◽  
RLN Harris
Keyword(s):  
Amino Acid ◽  
Stability Constants ◽  
Metal Binding ◽  
Acid Group ◽  
Biologically Active ◽  
Amino Acid Group ◽  
Dimeric Complexes ◽  
Major Species ◽  
Active Amino Acid ◽  
Related Compounds

Complex formation of the biologically active amino acid L-mimosine [α-amino-β-(3-hydroxy-4-oxo-1,4-dihydropyridin-1-yl)propanoic acid (1)], mimosinic acid (2), mimosine methyl ether (9) and 3-hydroxy-1-methylpyridin-4(1H)-one (4) with Cu2+, Zn2+, Cd2+ and Pb2+ was studied. Stability constants were determined by potentiometric titration in 0.15M KNOB3 as inert electrolyte at 37�. In the monomeric complexes formed by the mimosine derivatives, metal binding by the hydroxypyridone moiety was favoured relative to the amino acid group. With mimosine, dimeric complexes were major species. Under physiological conditions, mimosine binds copper and zinc ions more strongly than do simpler amino acids.

scholarly journals Glutamic acid as green and bio-based α-amino acid catalyst promoted one-pot access to polyfunctionalized dihydro-2-oxypyrroles

2019 ◽  
Vol 84 (10) ◽  
pp. 1083-1092 ◽  
Author(s):  
Farzaneh Mohamadpour
Keyword(s):  
Amino Acid ◽  
Glutamic Acid ◽  
Acid Catalyst ◽  
Biologically Active ◽  
Domino Reaction ◽  
Solid Catalyst ◽  
Reaction Conditions ◽  
One Pot ◽  
Active Amino Acid ◽  
Work Up

A highly versatile and convenient synthetic route for biologically active ?-amino acid, glutamic acid catalyzed facile and mild preparation of polyfunctionalized dihydro-2-oxypyrroles via one-pot, four condensation domino reaction between aromatic/aliphatic amines, dialkyl acetylenedicarboxylates and formaldehyde have been studied. The route includes green, biodegradable and inexpensive ?-amino acid catalyst, high atom-economy, simplicity of operation and work-up procedures, without chromatographic purification steps. The solid catalyst, non-toxic or hazardous, easily handled with mild reaction conditions and excellent yields are the notable benefits of the highly efficient and expedient synthesis of these products.

Application of surface active amino acid ionic liquids as phase-transfer catalyst

2020 ◽  
Vol 303 ◽  
pp. 112607 ◽  
Author(s):  
Emil Szepiński ◽  
Patrycja Smolarek ◽  
Maria J. Milewska ◽  
Justyna Łuczak
Keyword(s):  
Ionic Liquids ◽  
Amino Acid ◽  
Phase Transfer ◽  
Phase Transfer Catalyst ◽  
Active Amino Acid ◽  
Surface Active

Predicting the Strength of Stacking Interactions Between Heterocycles and Aromatic Amino Acid Side Chains

2019 ◽  
Author(s):  
Andrea N. Bootsma ◽  
Analise C. Doney ◽  
Steven Wheeler
Keyword(s):  
Amino Acid ◽  
Binding Sites ◽  
Aromatic Amino Acid ◽  
Aromatic Amino Acids ◽  
Biologically Active ◽  
Side Chains ◽  
Stacking Interactions ◽  
Inhibitor Binding ◽  
Protein Binding Sites ◽  
Amino Acid Side Chains

<p>Despite the ubiquity of stacking interactions between heterocycles and aromatic amino acids in biological systems, our ability to predict their strength, even qualitatively, is limited. Based on rigorous <i>ab initio</i> data, we have devised a simple predictive model of the strength of stacking interactions between heterocycles commonly found in biologically active molecules and the amino acid side chains Phe, Tyr, and Trp. This model provides rapid predictions of the stacking ability of a given heterocycle based on readily-computed heterocycle descriptors. We show that the values of these descriptors, and therefore the strength of stacking interactions with aromatic amino acid side chains, follow simple predictable trends and can be modulated by changing the number and distribution of heteroatoms within the heterocycle. This provides a simple conceptual model for understanding stacking interactions in protein binding sites and optimizing inhibitor binding in drug design.</p>

Analogues of the cholecystokinin octapeptide modified in the central part of the molecule

1991 ◽  
Vol 56 (9) ◽  
pp. 1963-1970 ◽  
Author(s):  
Jan Hlaváček ◽  
Václav Čeřovský ◽  
Jana Pírková ◽  
Pavel Majer ◽  
Lenka Maletínská ◽  
...  
Keyword(s):  
Amino Acid ◽  
Biological Activities ◽  
Point Of View ◽  
Biologically Active ◽  
Side Chain ◽  
Amino Acid Residues ◽  
Cholecystokinin Octapeptide ◽  
Biological Tests ◽  
Biological Potency ◽  
Biologically Active Conformation

In a series of analogues of the cholecystokinin octapeptide (CCK-8) the amino acid residues were gradually modified by substituting Gly by Pro in position 4, Trp by His in position 5, Met by Cle in position 6, or the Gly residue was inserted between Tyr and Met in positions 2 and 3 of the peptide chain, and in the case of the cholecystokinin heptapeptide (CCK-7) the Met residues were substituted by Nle or Aib. These peptides were investigated from the point of view of their biological potency in the peripheral and central region. From the results of the biological tests it follows that the modifications carried out in these analogues and in their Nα-Boc derivatives mean a suppression of the investigated biological activities by 2-3 orders of magnitude (at a maximum dose of the tested substance of 2 . 10-2 mg per animal).This means that a disturbance of the assumed biologically active conformation of CCK-8, connected with a considerable decrease of the biological potency of the molecule, takes place not only after introduction of the side chain into its centre (substitution of Gly4), but also after the modification of the side chains of the amino acids or by extension of the backbone in further positions around this central amino acid.

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