Stepwise synthesis of oligopeptides withN-carboxy ?-amino acid anhydrides. II. Oligopeptides with some polar side chains

Biopolymers ◽  
1971 ◽  
Vol 10 (11) ◽  
pp. 2199-2208 ◽  
Author(s):  
Ryoichi Katakai ◽  
Masanao Oya ◽  
Keikichi Uno ◽  
Yoshio Iwakura
Keyword(s):  
Amino Acid ◽  
Side Chains ◽  
Stepwise Synthesis ◽  
Acid Anhydrides

Stepwise synthesis of oligopeptides withN-carboxy ?-amino acid anhydrides

Biopolymers ◽  
1970 ◽  
Vol 9 (12) ◽  
pp. 1419-1427 ◽  
Author(s):  
Oshio Iwakura ◽  
Keikichi Uno ◽  
Masanao Oya ◽  
Ryoichi Katakai
Keyword(s):  
Amino Acid ◽  
Stepwise Synthesis ◽  
Acid Anhydrides

Stepwise synthesis of oligopeptides with N-carboxy-.alpha.-amino acid anhydrides. IV. N-Carboxyglycine anhydride

1972 ◽  
Vol 37 (2) ◽  
pp. 327-329 ◽  
Author(s):  
Ryoichi. Katakai ◽  
Masanao. Oya ◽  
Keikichi. Uno ◽  
Yoshio. Iwakura
Keyword(s):  
Amino Acid ◽  
Stepwise Synthesis ◽  
Acid Anhydrides ◽  
Alpha Amino Acid

Predicting the Strength of Stacking Interactions Between Heterocycles and Aromatic Amino Acid Side Chains

2019 ◽  
Author(s):  
Andrea N. Bootsma ◽  
Analise C. Doney ◽  
Steven Wheeler
Keyword(s):  
Amino Acid ◽  
Binding Sites ◽  
Aromatic Amino Acid ◽  
Aromatic Amino Acids ◽  
Biologically Active ◽  
Side Chains ◽  
Stacking Interactions ◽  
Inhibitor Binding ◽  
Protein Binding Sites ◽  
Amino Acid Side Chains

<p>Despite the ubiquity of stacking interactions between heterocycles and aromatic amino acids in biological systems, our ability to predict their strength, even qualitatively, is limited. Based on rigorous <i>ab initio</i> data, we have devised a simple predictive model of the strength of stacking interactions between heterocycles commonly found in biologically active molecules and the amino acid side chains Phe, Tyr, and Trp. This model provides rapid predictions of the stacking ability of a given heterocycle based on readily-computed heterocycle descriptors. We show that the values of these descriptors, and therefore the strength of stacking interactions with aromatic amino acid side chains, follow simple predictable trends and can be modulated by changing the number and distribution of heteroatoms within the heterocycle. This provides a simple conceptual model for understanding stacking interactions in protein binding sites and optimizing inhibitor binding in drug design.</p>

A Strategy for Thioamide Incorporation During Fmoc Solid-Phase Peptide Synthesis with Robust Stereochemical Integrity

2019 ◽  
Author(s):  
luis camacho III ◽  
Bryan J. Lampkin ◽  
Brett VanVeller
Keyword(s):  
Amino Acid ◽  
Functional Groups ◽  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Side Chains ◽  
Amino Acid Side Chains ◽  
Peptide Elongation

We describe a method to protect the sensitive stereochemistry of the thioamide—in analogy to the protection of the functional groups of amino acid side chains—in order to preserve the thioamide moiety during peptide elongation.<br>

Infrared spectra of N-acetyl-L-α-amino-acid N'-methylamides with aliphatic side chains in non-polar solvents

1981 ◽  
Vol 46 (3) ◽  
pp. 772-780 ◽  
Author(s):  
Jorga Smolíková ◽  
Jan Pospíšek ◽  
Karel Bláha
Keyword(s):  
Amino Acid ◽  
Conformational Changes ◽  
Infrared Spectra ◽  
Room Temperature ◽  
Side Chains ◽  
Polar Solvents

Infrared spectra of the L-alanine (I), L-leucine (II), L-valine (III) and L-tert-leucine (IV) N-acetyl N'-methylamides were measured. Amides I-IV are not self associated in tetrachlormethane in the concentration 2 . 10-5 mol l-1 at room temperature and in tetrachloroethylene in the concentration 1.5 . 10-4 mol l-1 at temperatures above 65° C. True conformational changes are observable only with the least flexible amide IV which exists at room temperature in a C5 conformation. This conformational type is also highly populated in the valine derivative III, but is less important in the alanine and leucine derivatives I and II in which the intramolecularly bonded C7 and the distorted hydrogen-nonbonded conformations contribute seriously.

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 Mobile unnatural amino acid side chains in the core of staphylococcal nuclease

1996 ◽  
Vol 5 (6) ◽  
pp. 1026-1031 ◽  
Author(s):  
Richard Wynn ◽  
Paul C. Harkins ◽  
Frederic M. Richards ◽  
Robert O. Fox
Keyword(s):  
Amino Acid ◽  
Staphylococcal Nuclease ◽  
Unnatural Amino Acid ◽  
Side Chains ◽  
The Core ◽  
Amino Acid Side Chains
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