A simple method for the preparation of functionalized trisubstituted alkenes and α,β,γ,δ-unsaturated carbonyl compounds by using natural amino acid l-tryptophan

2010 ◽  
Vol 11 (7) ◽  
pp. 656-659 ◽  
Author(s):  
Ying Hu ◽  
Yan-Hong He ◽  
Zhi Guan
Keyword(s):  
Amino Acid ◽  
Carbonyl Compounds ◽  
Natural Amino Acid ◽  
Simple Method ◽  
Trisubstituted Alkenes

scholarly journals Beneficial Impacts of Incorporating the Non-Natural Amino Acid Azulenyl-Alanine into the Trp-Rich Antimicrobial Peptide buCATHL4B

Biomolecules ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 421
Author(s):  
Areetha R. D’Souza ◽  
Matthew R. Necelis ◽  
Alona Kulesha ◽  
Gregory A. Caputo ◽  
Olga V. Makhlynets
Keyword(s):  
Amino Acid ◽  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Mechanism Of Action ◽  
Bactericidal Activity ◽  
Antimicrobial Agents ◽  
Human Cells ◽  
Side Chains ◽  
Natural Amino Acid ◽  
Proteolytic Stability

Antimicrobial peptides (AMPs) present a promising scaffold for the development of potent antimicrobial agents. Substitution of tryptophan by non-natural amino acid Azulenyl-Alanine (AzAla) would allow studying the mechanism of action of AMPs by using unique properties of this amino acid, such as ability to be excited separately from tryptophan in a multi-Trp AMPs and environmental insensitivity. In this work, we investigate the effect of Trp→AzAla substitution in antimicrobial peptide buCATHL4B (contains three Trp side chains). We found that antimicrobial and bactericidal activity of the original peptide was preserved, while cytocompatibility with human cells and proteolytic stability was improved. We envision that AzAla will find applications as a tool for studies of the mechanism of action of AMPs. In addition, incorporation of this non-natural amino acid into AMP sequences could enhance their application properties.

Sodium borohydride: A versatile reagent in the reductive N-monoalkylation of α-amino acids and α-amino methyl esters

2002 ◽  
Vol 80 (7) ◽  
pp. 779-788 ◽  
Author(s):  
Giancarlo Verardo ◽  
Paola Geatti ◽  
Elena Pol ◽  
Angelo G Giumanini
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Sodium Borohydride ◽  
Carbonyl Compounds ◽  
Condensation Reaction ◽  
Methyl Esters ◽  
Reducing Agent ◽  
Reductive Condensation ◽  
Versatile Reagent

α-Amino acids and α-amino methyl esters are easily converted to their N-monoalkyl derivatives by a reductive condensation reaction using several carbonyl compounds in the presence of sodium borohydride. This reducing agent has shown a wide versatility with minor but essential procedural variations. The reaction allows the α-monodeuterium labeling of the new N-substituent by use of sodium borodeuteride.Key words: α-amino acid, α-amino methyl esters, sodium borohydride, reductive N-monoalkylation, carbonyl compounds.

scholarly journals Structure–activity relationships of natural and non-natural amino acid-based amide and 2-oxoamide inhibitors of human phospholipase A2 enzymes

2008 ◽  
Vol 16 (24) ◽  
pp. 10257-10269 ◽  
Author(s):  
Georgia Antonopoulou ◽  
Efrosini Barbayianni ◽  
Victoria Magrioti ◽  
Naomi Cotton ◽  
Daren Stephens ◽  
...  
Keyword(s):  
Amino Acid ◽  
Phospholipase A2 ◽  
Natural Amino Acid ◽  
Structure Activity Relationships ◽  
Structure Activity

scholarly journals Rapid purification and characterization of human platelet glycoprotein V: the amino acid sequence contains leucine-rich repetitive modules as in glycoprotein Ib

Blood ◽  
1990 ◽  
Vol 75 (12) ◽  
pp. 2349-2356 ◽  
Author(s):  
T Shimomura ◽  
K Fujimura ◽  
S Maehama ◽  
M Takemoto ◽  
K Oda ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Structural Model ◽  
Consensus Sequence ◽  
Reversed Phase ◽  
Platelet Glycoprotein ◽  
Lectin Affinity Chromatography ◽  
Glycoprotein Ib ◽  
Simple Method ◽  
Carbohydrate Chains

Glycoprotein V (GPV) is a membrane-associated, 82 Kd platelet glycoprotein that is hydrolyzed during thrombin activation to yield 69 Kd fragment. We have developed a rapid and simple method for isolation of the protein from platelet extracts using a combination of gel permeation, anion-exchange, and lectin affinity chromatography. The partial amino acid sequence was determined by analysis of peptides generated by digestion of the S-carboxyamido-methylated protein with Achromobacter protease I or cyanogen bromide. The sequence shows a remarkable periodicity of leucine residues, which is homologous to the consensus sequence of a highly diversified protein super-family with a common repetitive module. Thrombin cleavage site was determined to be located at the C-terminal region of GPV by analysis of the products separated by sizing and reversed-phase high performance liquid chromatography. By lectin blot analysis, the existence of mucin-type carbohydrate chains was indicated, as well as the existence of asparagine-linked carbohydrate chains shown by the amino acid sequence analysis. From these data, we report a structural model of GPV that is analogous to glycoprotein Ib.

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