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

Helix formation in ε-amino acid oligomers

2009 ◽  
Vol 907 (1-3) ◽  
pp. 109-114 ◽  
Author(s):  
Peter Schramm ◽  
Hans-Jörg Hofmann
Keyword(s):  
Amino Acid ◽  
Helix Formation ◽  
Amino Acid Oligomers

ChemInform Abstract: Helix Formation in ε-Amino Acid Oligomers

ChemInform ◽  
2010 ◽  
Vol 41 (10) ◽  
Author(s):  
Peter Schramm ◽  
Hans-Joerg Hofmann
Keyword(s):  
Amino Acid ◽  
Helix Formation ◽  
Amino Acid Oligomers

Unique Functional Materials Derived from β-Amino Acid Oligomers

2017 ◽  
Vol 70 (2) ◽  
pp. 126 ◽  
Author(s):  
Mark P. Del Borgo ◽  
Ketav Kulkarni ◽  
Marie-Isabel Aguilar
Keyword(s):  
Amino Acid ◽  
Drug Design ◽  
Self Assembly ◽  
Functional Materials ◽  
Bioactive Molecules ◽  
Peptide Drug ◽  
New Materials ◽  
Amino Acid Oligomers

The unique structures formed by β-amino acid oligomers, or β-peptide foldamers, have been studied for almost two decades, which has led to the discovery of several distinctive structures and bioactive molecules. Recently, this area of research has expanded from conventional peptide drug design to the formation of assemblies and nanomaterials by peptide self-assembly. The unique structures formed by β-peptides give rise to a set of new materials with altered properties that differ from conventional peptide-based materials; such new materials may be useful in several bio- and nanomaterial applications.

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.

Robust Helix Formation in a New Family of Oligoureas Based on a Constrained Bicyclic Building Block

2012 ◽  
Vol 124 (45) ◽  
pp. 11429-11432 ◽  
Author(s):  
Baptiste Legrand ◽  
Christophe André ◽  
Emmanuel Wenger ◽  
Claude Didierjean ◽  
Marie Christine Averlant-Petit ◽  
...  
Keyword(s):  
Building Block ◽  
New Family ◽  
Helix Formation

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

SECONDARY STRUCTURAL INVESTIGATIONS OF NOVEL OXETANE AMINO ACID OLIGOMERS

2002 ◽  
Author(s):  
Donald Angus ◽  
Sarah Barker ◽  
Timothy D. W. Claridge ◽  
George W. J. Fleet ◽  
Victoria Gomez ◽  
...  
Keyword(s):  
Amino Acid ◽  
Structural Investigations ◽  
Amino Acid Oligomers

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.

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