Computational Study of the Stability of Natural Amino Acid isomers

2021 ◽  
Author(s):  
Stefano Crespi ◽  
Dhanalakshmi Vadivel ◽  
Alfredo Bellisario ◽  
Daniele Dondi
Keyword(s):  
Amino Acid ◽  
Computational Study ◽  
Natural Amino Acid ◽  
The Stability

scholarly journals Alteration in H-bond strength affects the stability of codon-anticodon interaction at in-frame UAG stop codon during in vitro translation

2021 ◽  
Author(s):  
Purnima Mala ◽  
Ishu Saraogi
Keyword(s):  
Amino Acid ◽  
Stop Codon ◽  
Protein Translation ◽  
In Vitro Translation ◽  
Natural Amino Acid ◽  
Additional Hydrogen Bond ◽  
Amino Acid Mutagenesis ◽  
The Stability ◽  
Decoding Ability

We have studied the decoding ability of a non-standard nucleobase modified tRNA for non-natural amino acid mutagenesis. The insertion of 2, 6-diaminopurine (D) base at the 3rd position of a tRNA anticodon enabled us to evaluate the effect of an additional hydrogen bond during translation. The presence of D at the tRNA anticodon led to stabilization of the codon-anticodon interaction due to an additional H-bond between the N2-exocyclic amine of D and the C2 carbonyl group of uracil during protein translation. While decoding UAG codons using stop codon suppression methodology, the enhanced codon-anticodon interaction improved codon readthrough and synthesis of modified protein with a non-natural amino acid at multiple sites. Our findings imply that the number of hydrogen bonds at the tRNA-mRNA duplex interface is an important criterion during mRNA decoding and improves protein translation at multiple UAG stop sites. This work provides valuable inputs towards improved non-natural amino acid mutagenesis for creating functional proteins.

scholarly journals Alteration in H-bond strength affects the stability of codon-anticodon interaction at in-frame UAG stop codon during in vitro translation

2021 ◽  
Author(s):  
Purnima Mala ◽  
Ishu Saraogi
Keyword(s):  
Amino Acid ◽  
Stop Codon ◽  
Protein Translation ◽  
In Vitro Translation ◽  
Natural Amino Acid ◽  
Additional Hydrogen Bond ◽  
Amino Acid Mutagenesis ◽  
The Stability ◽  
Decoding Ability

We have studied the decoding ability of a non-standard nucleobase modified tRNA for non-natural amino acid mutagenesis. The insertion of 2, 6-diaminopurine (D) base at the 3rd position of a tRNA anticodon enabled us to evaluate the effect of an additional hydrogen bond during translation. The presence of D at the tRNA anticodon led to stabilization of the codon-anticodon interaction due to an additional H-bond between the N2-exocyclic amine of D and the C2 carbonyl group of uracil during protein translation. While decoding UAG codons using stop codon suppression methodology, the enhanced codon-anticodon interaction improved codon readthrough and synthesis of modified protein with a non-natural amino acid at multiple sites. Our findings imply that the number of hydrogen bonds at the tRNA-mRNA duplex interface is an important criterion during mRNA decoding and improves protein translation at multiple UAG stop sites. This work provides valuable inputs towards improved non-natural amino acid mutagenesis for creating functional proteins.

CORTICOTROPHIC EFFECT OF SYNTHETIC ACTH-PEPTIDES WITH NATURAL AMINO ACID SEQUENCE OF DIFFERENT CHAIN LENGTH IN COMPARISON TO THEIR D-SER1-DERIVATIVES

1971 ◽  
Vol 68 (1_Supplb) ◽  
pp. S48
Author(s):  
P. L. Barthe ◽  
L. Schenkel-Hulliger ◽  
W. Rittel ◽  
P. A. Desaulles
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Chain Length ◽  
Natural Amino Acid

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.

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
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