ChemInform Abstract: FMOC-Protected Tropane-Based Amino Acids for Peptide Structure- Function Studies

ChemInform ◽  
2010 ◽  
Vol 28 (31) ◽  
pp. no-no
Author(s):  
P. E. THOMPSON ◽  
M. T. W. HEARN
Keyword(s):  
Amino Acids ◽  
Structure Function ◽  
Peptide Structure

Fmoc-protected tropane-based amino acids for peptide structure-function studies

1997 ◽  
Vol 38 (16) ◽  
pp. 2907-2910 ◽  
Author(s):  
Philip E. Thompson ◽  
Milton T.W. Hearn
Keyword(s):  
Amino Acids ◽  
Structure Function ◽  
Peptide Structure

Tropane-based amino acids for peptide structure-function studies: Inhibitors of platelet aggregation

1998 ◽  
Vol 8 (19) ◽  
pp. 2699-2704 ◽  
Author(s):  
Philip E Thompson ◽  
David L Steer ◽  
Marie-Isabel Aguilar ◽  
Milton T.W. Hearn
Keyword(s):  
Amino Acids ◽  
Platelet Aggregation ◽  
Structure Function ◽  
Peptide Structure

ChemInform Abstract: Tropane-Based Amino Acids for Peptide Structure-Function Studies: Inhibitors of Platelet Aggregation.

ChemInform ◽  
2010 ◽  
Vol 30 (8) ◽  
pp. no-no
Author(s):  
P. E. THOMPSON ◽  
D. L. STEER ◽  
M.-I. AGUILAR ◽  
M. T. W. HEARN
Keyword(s):  
Amino Acids ◽  
Platelet Aggregation ◽  
Structure Function ◽  
Peptide Structure

Exploration of the forbidden regions of the Ramachandran plot (ϕ-ψ) with QTAIM

2017 ◽  
Vol 19 (38) ◽  
pp. 26423-26434 ◽  
Author(s):  
Roya Momen ◽  
Alireza Azizi ◽  
Lingling Wang ◽  
Yang Ping ◽  
Tianlv Xu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Peptide Structure ◽  
Ramachandran Plot ◽  
Left Response ◽  
Forbidden Regions ◽  
Dark Green ◽  
Ramachandran Plots ◽  
Pale Green

Left: Response β is defined as: β = arccos(e̲2·y̲) with β* = arccos(e̲1·y̲). Right: QTAIM interpreted Ramachandran plots {(βϕ,βϕ*)-(βψ,βψ*)} ‘-’ is a hyphen and not a subtraction sign. Pale green and dark green crosses indicate the glycine, pink and red pluses represent the remaining amino acids (a.a.) in the magainin peptide structure.

scholarly journals Stapled Peptides—A Useful Improvement for Peptide-Based Drugs

Molecules ◽  
2019 ◽  
Vol 24 (20) ◽  
pp. 3654 ◽  
Author(s):  
Mattia Moiola ◽  
Misal G. Memeo ◽  
Paolo Quadrelli
Keyword(s):  
Amino Acids ◽  
Scientific Community ◽  
Peptide Structure ◽  
Peptide Drug ◽  
Cross Link ◽  
Stapled Peptides ◽  
New Techniques ◽  
Low Degree ◽  
Drug Synthesis ◽  
The Right

Peptide-based drugs, despite being relegated as niche pharmaceuticals for years, are now capturing more and more attention from the scientific community. The main problem for these kinds of pharmacological compounds was the low degree of cellular uptake, which relegates the application of peptide-drugs to extracellular targets. In recent years, many new techniques have been developed in order to bypass the intrinsic problem of this kind of pharmaceuticals. One of these features is the use of stapled peptides. Stapled peptides consist of peptide chains that bring an external brace that force the peptide structure into an α -helical one. The cross-link is obtained by the linkage of the side chains of opportune-modified amino acids posed at the right distance inside the peptide chain. In this account, we report the main stapling methodologies currently employed or under development and the synthetic pathways involved in the amino acid modifications. Moreover, we report the results of two comparative studies upon different kinds of stapled-peptides, evaluating the properties given from each typology of staple to the target peptide and discussing the best choices for the use of this feature in peptide-drug synthesis.

scholarly journals Regulated nuclear import of the Drosophila rel protein dorsal: structure-function analysis.

1996 ◽  
Vol 16 (3) ◽  
pp. 1103-1114 ◽  
Author(s):  
S Govind ◽  
E Drier ◽  
L H Huang ◽  
R Steward
Keyword(s):  
Amino Acids ◽  
Structure Function ◽  
Nuclear Localization ◽  
Nuclear Import ◽  
Function Analysis ◽  
Drosophila Embryo ◽  
Nuclear Targeting ◽  
Homology Region ◽  
Early Drosophila Embryo

The formation of a gradient of nuclear Dorsal protein in the early Drosophila embryo is the last step in a maternally encoded dorsal-ventral signal transduction pathway. This gradient is formed in response to a ventral signal, which leads to the dissociation of cytoplasmic Dorsal from the I kappa B homolog Cactus. Free Dorsal is then targeted to the nucleus. Dorsal is a Rel-family transcription factor. Signal-dependent nuclear localization characterizes the regulation of Rel proteins. In order to identify regions of Dorsal that are essential for its homodimerization, nuclear targeting, and interaction with Cactus, we have performed an in vivo structure-function analysis. Our results show that all these functions are carried out by regions within the conserved Rel-homology region of Dorsal. The C-terminal divergent half of Dorsal is dispensable for its selective nuclear import. A basic stretch of 6 amino acids at the C terminus of the Rel-homology region is necessary for nuclear localization. This nuclear localization signal is not required for Cactus binding. Removal of the N-terminal 40 amino acids abolished the nuclear import of Dorsal, uncovering a potentially novel function for this highly conserved region.

Structure-function relationships of peptide fragments of gastrin and cholecystokinin.

1977 ◽  
Vol 233 (4) ◽  
pp. E286
Author(s):  
D L Kaminski ◽  
M J Ruwart ◽  
M Jellinek
Keyword(s):  
Amino Acids ◽  
Structure Function ◽  
Bile Flow ◽  
Hydrogen Ion ◽  
Biliary System ◽  
Peptide Fragments ◽  
Hepatic Bile ◽  
Amino Acid Peptide ◽  
The Common ◽  
Active Fragments

This study evaluates the structure-function relationships of the C-terminal peptide fragments of gastrin and cholecystokinin (CCK) in the biliary system and the stomach. Dogs with chronic biliary and gastric fistulas were used. Administration of the common fragments of CCK and gastrin with four and five amino acids and the active fragments of CCK with six through eight amino acids without sulfation of tyrosine in position 7 failed to alter hepatic bile flow from control values while significantly stimulating gastric hydrogen ion output. Administration of the seven and eight amino acid peptide fragments of CCK with sulfation of tyrosine in position 7 significantly increased hepatic bile flow. Administration of the sulfated octapeptide with 4 microgram/kg per h of nonsulfated octapeptide did not result in the inhibition of the choleresis produced by the sulfated peptide. The gastric hydrogen ion response produced by the administration of the nonsulfated and sulfated peptide was equal to that of the nonsulfated peptide alone. These results suggest that in the biliary system the receptor is highly specific as sulfation of the peptide fragment of CCK is essential for combining with the receptor, whereas in the stomach the receptor has little specificity and combines with all of the peptide fragments evaluated.

scholarly journals Escherichia coli amino acid auxotrophic expression host strains for investigating protein structure-function relationships

2020 ◽  
Author(s):  
Toshio Iwasaki ◽  
Yoshiharu Miyajima-Nakano ◽  
Risako Fukazawa ◽  
Myat T Lin ◽  
Shin-Ichi Matsushita ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Protein Structure ◽  
Amino Acid ◽  
Structure Function ◽  
Growth Medium ◽  
Isotope Labeling ◽  
Water Soluble ◽  
Expression Host ◽  
Host Strains

Abstract A set of C43(DE3) and BL21(DE3) Escherichia coli host strains that are auxotrophic for various amino acids is briefly reviewed. These strains require the addition of a defined set of one or more amino acids in the growth medium, and have been specifically designed for overproduction of membrane or water-soluble proteins selectively labeled with stable isotopes such as 2H, 13C and 15N. The strains described here are available for use and have been deposited into public strain banks. Although they cannot fully eliminate the possibility of isotope dilution and mixing, metabolic scrambling of the different amino acid types can be minimized through a careful consideration of the bacterial metabolic pathways. The use of a suitable auxotrophic expression host strain with an appropriately isotopically labeled growth medium ensures high levels of isotope labeling efficiency as well as selectivity for providing deeper insight into protein structure-function relationships.

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