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

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.

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

Isolation, folding and structural investigations of the amino acid transporter OEP16

2011 ◽  
Vol 80 (2) ◽  
pp. 157-168 ◽  
Author(s):  
Da Qun Ni ◽  
James Zook ◽  
Douglas A. Klewer ◽  
Ronald A. Nieman ◽  
J. Soll ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Transporter ◽  
Structural Investigations ◽  
Acid Transporter

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

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

scholarly journals Structural Investigations of a New Familial Dysalbuminemic Hyperthyroxinemia Genotype

1999 ◽  
Vol 45 (8) ◽  
pp. 1248-1254 ◽  
Author(s):  
Charles E Petersen ◽  
Chung-Eun Ha ◽  
Krishna Harohalli ◽  
David S Park ◽  
Jimmy B Feix ◽  
...  
Keyword(s):  
Amino Acid ◽  
Human Serum Albumin ◽  
Dissociation Constants ◽  
High Serum ◽  
Wild Type ◽  
Japanese Family ◽  
Structural Investigations ◽  
Kd Values ◽  
Total Thyroxine ◽  
Caucasian Patients

Abstract Background: In a previous study, we found that the amino acid substitution R218H in human serum albumin (HSA) was the cause of familial dysalbuminemic hyperthyroxinemia (FDH) in several Caucasian patients. Subsequently the substitution R218P was shown to be the cause of FDH in several members of a Japanese family. This study attempts to resolve discrepancies in the only other study of R218P HSA and identifies two new Japanese R218P FDH patients unrelated to those described previously. Methods and Results: Recombinant R218H, R218P, and wild-type HSA were synthesized in yeast, and the affinities of these HSA species for l- and d-thyroxine were determined using fluorescence spectroscopy. The dissociation constants for the binding of wild-type, R218P, and R218H HSA to l-thyroxine were 1.44 × 10−6, 2.64 × 10−7, and 2.49 × 10−7 mol/L, respectively. The circular dichroism spectra of thyroxine bound to R218H and R218P HSA were markedly different, indicating that the structure of the thyroxine/HSA complex is different for either protein. Conclusions: The Kd values for l-thyroxine bound to R218P and R218H HSA determined in this study were similar. The extremely high serum total-thyroxine concentrations reported previously for R218P FDH patients (10-fold higher than those reported for R218H FDH patients) are not consistent with the Kd values determined in this study. Possible explanations for these discrepancies are discussed.

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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