Insertion of oximic and hydroxamic functions into one simple amino acid creates a new family of powerful chelating agents

1998 ◽  
pp. 1089-1090 ◽  
Author(s):  
Agnieszka Dobosz ◽  
Igor O. Fritsky ◽  
Aldona Karaczyn ◽  
Henryk Kozłowski ◽  
Tatiana Yu. Sliva ◽  
...  
Keyword(s):  
Amino Acid ◽  
Chelating Agents ◽  
New Family ◽  
Simple Amino Acid

scholarly journals Hybrid Cyclobutane/Proline-Containing Peptidomimetics: The Conformational Constraint Influences Their Cell-Penetration Ability

2021 ◽  
Vol 22 (10) ◽  
pp. 5092
Author(s):  
Ona Illa ◽  
Jimena Ospina ◽  
José-Emilio Sánchez-Aparicio ◽  
Ximena Pulido ◽  
María Ángeles Abengozar ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cell Penetrating Peptides ◽  
Cell Uptake ◽  
Relevant Parameter ◽  
Intracellular Accumulation ◽  
Peptide Backbone ◽  
New Family ◽  
Cell Line Hela ◽  
Penetration Ability ◽  
Tumoral Cell

A new family of hybrid β,γ-peptidomimetics consisting of a repetitive unit formed by a chiral cyclobutane-containing trans-β-amino acid plus a Nα-functionalized trans-γ-amino-l-proline joined in alternation were synthesized and evaluated as cell penetrating peptides (CPP). They lack toxicity on the human tumoral cell line HeLa, with an almost negligible cell uptake. The dodecapeptide showed a substantial microbicidal activity on Leishmania parasites at 50 µM but with a modest intracellular accumulation. Their previously published γ,γ-homologues, with a cyclobutane γ-amino acid, showed a well-defined secondary structure with an average inter-guanidinium distance of 8–10 Å, a higher leishmanicidal activity as well as a significant intracellular accumulation. The presence of a very rigid cyclobutane β-amino acid in the peptide backbone precludes the acquisition of a defined conformation suitable for their cell uptake ability. Our results unveiled the preorganized charge-display as a relevant parameter, additional to the separation among the charged groups as previously described. The data herein reinforce the relevance of these descriptors in the design of CPPs with improved properties.

Amino Acid Conjugated Sophorolipids:  A New Family of Biologically Active Functionalized Glycolipids

2006 ◽  
Vol 17 (6) ◽  
pp. 1523-1529 ◽  
Author(s):  
Abul Azim ◽  
Vishal Shah ◽  
Gustavo F. Doncel ◽  
Nicholas Peterson ◽  
Wei Gao ◽  
...  
Keyword(s):  
Amino Acid ◽  
Biologically Active ◽  
New Family

scholarly journals Metal self-assembly mimosine peptides with enhanced antimicrobial activity: towards a new generation of multitasking chelating agents

2020 ◽  
Vol 49 (9) ◽  
pp. 2862-2879 ◽  
Author(s):  
Joanna Izabela Lachowicz ◽  
Gabriele Dalla Torre ◽  
Rosita Cappai ◽  
Enrico Randaccio ◽  
Valeria M. Nurchi ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Self Assembly ◽  
Building Block ◽  
Chelating Agents ◽  
Metal Coordination ◽  
Protein Amino Acid ◽  
Coordination Ability ◽  
New Generation

Mimosine is a non-protein amino acid that can be used as a building block in peptides with metal coordination ability.

Oxidation Studies of Mn(III)–Amino Acid Chelating Agents

2012 ◽  
Vol 41 (11) ◽  
pp. 1937-1947 ◽  
Author(s):  
Ganesan Sivakumar ◽  
Nachimuthu Krishnaveni ◽  
Manickam Umayavalli
Keyword(s):  
Amino Acid ◽  
Chelating Agents

scholarly journals Peptidase E, a Peptidase Specific for N-Terminal Aspartic Dipeptides, Is a Serine Hydrolase

2000 ◽  
Vol 182 (9) ◽  
pp. 2536-2543 ◽  
Author(s):  
Rachel A. L. Lassy ◽  
Charles G. Miller
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Site Directed Mutagenesis ◽  
Amino Acid Residues ◽  
Serine Hydrolase ◽  
Genome Sequences ◽  
New Family ◽  
The Family ◽  
Serovar Typhimurium ◽  
Structural Classes

ABSTRACT Salmonella enterica serovar Typhimurium peptidase E (PepE) is an N-terminal Asp-specific dipeptidase. PepE is not inhibited by any of the classical peptidase inhibitors, and its amino acid sequence does not place it in any of the known peptidase structural classes. A comparison of the amino acid sequence of PepE with a number of related sequences has allowed us to define the amino acid residues that are strongly conserved in this family. To ensure the validity of this comparison, we have expressed one of the most distantly related relatives (Xenopus) in Escherichia coli and have shown that it is indeed an Asp-specific dipeptidase with properties very similar to those of serovar Typhimurium PepE. The sequence comparison suggests that PepE is a serine hydrolase. We have used site-directed mutagenesis to change all of the conserved Ser, His, and Asp residues and have found that Ser120, His157, and Asp135 are all required for activity. Conversion of Ser120 to Cys leads to severely reduced (104-fold) but still detectable activity, and this activity but not that of the parent is inhibited by thiol reagents; these results confirm that this residue is likely to be the catalytic nucleophile. These results suggest that PepE is the prototype of a new family of serine peptidases. The phylogenetic distribution of the family is unusual, since representatives are found in eubacteria, an insect (Drosophila), and a vertebrate (Xenopus) but not in the Archaea or in any of the other eukaryotes for which genome sequences are available.

scholarly journals The heterodimeric amino acid transporter 4F2hc/y+LAT2 mediates arginine efflux in exchange with glutamine

2000 ◽  
Vol 349 (3) ◽  
pp. 787-795 ◽  
Author(s):  
Angelika BRÖER ◽  
Carsten A. WAGNER ◽  
Florian LANG ◽  
Stefan BRÖER
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Mammalian Cells ◽  
Substrate Inhibition ◽  
Cell Types ◽  
Xenopus Laevis Oocytes ◽  
Cationic Amino Acid ◽  
New Family ◽  
Arginine Uptake ◽  
Intracellular Binding

The cationic amino acid arginine, due to its positive charge, is usually accumulated in the cytosol. Nevertheless, arginine has to be released by a number of cell types, e.g. kidney cells, which supply other organs with this amino acid, or the endothelial cells of the blood–brain barrier which release arginine into the brain. Arginine release in mammalian cells can be mediated by two different transporters, y+LAT1 and y+LAT2. For insertion into the plasma membrane, these transporters have to be associated with the type-II membrane glycoprotein 4F2hc [Torrents, Estevez, Pineda, Fernandez, Lloberas, Shi, Zorzano and Palacin (1998) J. Biol. Chem. 273, 32437–32445]. The present study elucidates the function and distribution of y+LAT2. In contrast to y+LAT1, which is expressed mainly in kidney epithelial cells, lung and leucocytes, y+LAT2 has a wider tissue distribution, including brain, heart, testis, kidney, small intestine and parotis. When co-expressed with 4F2hc in Xenopus laevis oocytes, y+LAT2 mediated uptake of arginine, leucine and glutamine. Arginine uptake was inhibited strongly by lysine, glutamate, leucine, glutamine, methionine and histidine. Mutual inhibition was observed when leucine or glutamine was used as substrate. Inhibition of arginine uptake by neutral amino acids depended on the presence of Na+, which is a hallmark of y+LAT-type transporters. Although arginine transport was inhibited strongly by glutamate, this anionic amino acid was only weakly transported by 4F2hc/y+LAT2. Amino acid transport via 4F2hc/y+LAT2 followed an antiport mechanism similar to the other members of this new family. Only preloaded arginine could be released in exchange for extracellular amino acids, whereas marginal release of glutamine or leucine was observed under identical conditions. These results indicated that arginine has the highest affinity for the intracellular binding site and that arginine release may be the main physiological function of this transporter.

β-Peptide Foldamers:  Robust Helix Formation in a New Family of β-Amino Acid Oligomers

1996 ◽  
Vol 118 (51) ◽  
pp. 13071-13072 ◽  
Author(s):  
Daniel H. Appella ◽  
Laurie A. Christianson ◽  
Isabella L. Karle ◽  
Douglas R. Powell ◽  
Samuel H. Gellman
Keyword(s):  
Amino Acid ◽  
New Family ◽  
Helix Formation ◽  
Amino Acid Oligomers
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