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

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

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.

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 New 19-Residue Peptaibols from Trichoderma Clade Viride

2018 ◽  
Vol 6 (3) ◽  
pp. 85 ◽  
Author(s):  
Tamás Marik ◽  
Chetna Tyagi ◽  
Gordana Racić ◽  
Dávid Rakk ◽  
András Szekeres ◽  
...  
Keyword(s):  
Amino Acid ◽  
Structural Investigation ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Helix Formation ◽  
Left Handed ◽  
Wall Structures ◽  
High Preference ◽  
Wide Range ◽  
Unusual Amino Acid

Trichoderma koningiopsis and T. gamsii belong to clade Viride of Trichoderma, the largest and most diverse group of this genus. They produce a wide range of bioactive secondary metabolites, including peptaibols with antibacterial, antifungal, and antiviral properties. The unusual amino acid residues of peptaibols, i.e., α-aminoisobutyric acid (Aib), isovaline (Iva), and the C-terminal 1,2-amino alcohol make them unique among peptides. In this study, the peptaibiomes of T. koningiopsis and T. gamsii were investigated by HPLC-ESI-MS. The examined strains appeared to produce 19-residue peptaibols, most of which are unknown from literature, but their amino acid sequences are similar to those of trikoningins, tricholongins, trichostrigocins, trichorzianins, and trichorzins. A new group of peptaibols detected in T. koningiopsis are described here under the name “Koningiopsin”. Trikoningin KA V, the closest peptaibol compound to the peptaibols produced by these two strains, was selected for structural investigation by short MD simulation, which revealed that many residues show high preference for left handed helix formation. The bioactivity of the peptaibol mixtures produced by T. koningiopsis and T. gamsii was tested on agar plates against bacteria, yeasts, and filamentous fungi. The results revealed characteristic differences in bioactivities towards the different groups of target microorganisms, which can be explained with the differences in their cell wall structures.

Amphipathic Helices from Aromatic Amino Acid Oligomers

2006 ◽  
Vol 71 (21) ◽  
pp. 7931-7939 ◽  
Author(s):  
Elizabeth R. Gillies ◽  
Christel Dolain ◽  
Jean-Michel Léger ◽  
Ivan Huc
Keyword(s):  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Amphipathic Helices ◽  
Amino Acid Oligomers

scholarly journals Helix Formation in Preorganized β/γ-Peptide Foldamers: Hydrogen-Bond Analogy to the α-Helix without α-Amino Acid Residues

2010 ◽  
Vol 132 (23) ◽  
pp. 7868-7869 ◽  
Author(s):  
Li Guo ◽  
Aaron M. Almeida ◽  
Weicheng Zhang ◽  
Andrew G. Reidenbach ◽  
Soo Hyuk Choi ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Amino Acid ◽  
Amino Acid Residues ◽  
Helix Formation ◽  
Α Helix

Impact of substituent effects on the design of β-sheet mimetics and β-double helices from (E)-vinylogous γ-amino acid oligomers

2019 ◽  
Vol 17 (41) ◽  
pp. 9226-9231
Author(s):  
Kuruva Veeresh ◽  
Manjeet Singh ◽  
Hosahudya N. Gopi
Keyword(s):  
Amino Acid ◽  
Substituent Effects ◽  
Double Helices ◽  
The Impact ◽  
Β Sheet ◽  
Amino Acid Oligomers

The impact of substituent effects at the γ-carbon on the structures of (E)-vinylogous γ-amino acid homooligomers is studied.

Isolation of microorganisms which utilize acidic d-amino acid oligomers

2001 ◽  
Vol 12 (1-6) ◽  
pp. 53-59 ◽  
Author(s):  
Yasuhisa Asano ◽  
Makiko Umezaki ◽  
Yong-Fu Li ◽  
Shuichirou Tsubota ◽  
Tina L Lübbehüsen
Keyword(s):  
Amino Acid ◽  
Amino Acid Oligomers
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