In-Peptide Synthesis of Imidazolidin-2-one Scaffolds, Equippable with Proteinogenic or Taggable/Linkable Side Chains, General Promoters of Unusual Secondary Structures

2019 ◽  
Vol 84 (9) ◽  
pp. 4992-5004 ◽  
Author(s):  
Rossella De Marco ◽  
Junwei Zhao ◽  
Arianna Greco ◽  
Simone Ioannone ◽  
Luca Gentilucci
Keyword(s):  
Peptide Synthesis ◽  
Secondary Structures ◽  
Side Chains

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>

An improved soluble polynorbornene support for peptide synthesis

RSC Advances ◽  
2015 ◽  
Vol 5 (113) ◽  
pp. 93027-93031
Author(s):  
Nimmashetti Naganna ◽  
Nandita Madhavan
Keyword(s):  
Peptide Synthesis ◽  
Side Chains ◽  
Coupling Reagents

A soluble polynorbornene support containing an oligoether linker as well as alkyl and oligoether side chains has been developed and used to synthesize Leu5-Enkephalin in 52% overall yield using only 1.2 equivalents of coupling reagents.

N-Methylamino Acids in Peptide Synthesis. II. A New Synthesis of N-Benzyloxycarbonyl, N-Methylamino Acids

1973 ◽  
Vol 51 (12) ◽  
pp. 1915-1919 ◽  
Author(s):  
John R. McDermott ◽  
N. Leo Benoiton
Keyword(s):  
Amino Acids ◽  
Methyl Iodide ◽  
Peptide Synthesis ◽  
Side Chains ◽  
Butyl Group ◽  
New Synthesis ◽  
Derivatives Of

Reaction of N-benzyloxycarbonyl derivatives of aliphatic amino acids, and threonine, aspartic, and glutamic acids whose side-chains were protected with the t-butyl group, gave the corresponding N-methylamino acid derivatives in good yields. The methionine derivative could be obtained by using only one mol of methyl iodide. Derivatives of threonine, and aspartic and glutamic acids whose side-chains were not protected could not be methylated. Analysis of the crude products of methylation in three cases showed that they contained 0–1% of racemized material.

scholarly journals Changes in Secondary Structures and Acidic Side Chains of Melibiose Permease upon Cosubstrates Binding

2006 ◽  
Vol 91 (12) ◽  
pp. 4440-4449 ◽  
Author(s):  
Xavier León ◽  
Raymonde Lemonnier ◽  
Gérard Leblanc ◽  
Esteve Padrós
Keyword(s):  
Secondary Structures ◽  
Side Chains

scholarly journals Two-dimensional infrared correlation spectroscopy studies on secondary structures and hydrogen bondings of side chains of proteins

2003 ◽  
Vol 17 (2-3) ◽  
pp. 79-100 ◽  
Author(s):  
Yukihiro Ozaki ◽  
Koichi Murayama ◽  
Yuqing Wu ◽  
Boguslawa Czarnik-Matusewicz
Keyword(s):  
Secondary Structures ◽  
Correlation Spectroscopy ◽  
Side Chains ◽  
Two Dimensional ◽  
2D Ir ◽  
Intensity Changes ◽  
Specific Order ◽  
Spectroscopy Studies ◽  
2D Correlation Spectroscopy ◽  
Hydrogen Bondings

This review paper reports usefulness of two-dimensional (2D) correlation spectroscopy in analyzing infrared (IR) spectra of proteins in aqueous solutions. In the 2D approach, spectral peaks are spread over the second dimension, thereby simplifying the visualization of complex spectra consisting of many overlapped bands, and enhancing spectral resolution. 2D correlation spectroscopy has a powerful deconvolution ability for highly overlapped amide I, amide II, and amide III bands of proteins, enabling these bands to be assigned to various secondary structures. It also provides the specific order of the spectral intensity changes taking place during the measurement on the value of controlling variable affecting the spectra. Therefore, one can monitor the order of secondary structure variations in proteins by using 2D IR correlation spectroscopy. 2D correlation spectroscopy also provides new insight into the hydrogen bondings of side chains of proteins. In this review the principles and advantages of 2D correlation spectroscopy are outlined first and then three examples of the applications of 2D IR spectroscopy to protein research are presented.

Synthesis and chiroptical properties of heterodetic cyclic hexapeptides related to oxytocin ring moiety

1980 ◽  
Vol 45 (4) ◽  
pp. 1109-1131 ◽  
Author(s):  
Ivo Frič ◽  
Lyudmila I. Leonteva ◽  
Petr Maloň ◽  
Karel Jošt ◽  
Karel Bláha
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Peptide Synthesis ◽  
Spatial Arrangement ◽  
Cd Spectroscopy ◽  
Side Chains ◽  
Peptide Backbone ◽  
Chiroptical Properties ◽  
Disulfide Group ◽  
Cyclic Hexapeptides

Cyclic disulfides of cysteinyl-tetraglycyl-cysteine (Ia), cysteinyl-tyrosyl-triglycyl-cysteine (Ib) and cysteinyl-tyrosyl-isoleucyl-diglycyl-cysteine (Ic) were synthesized by classical methods of peptide synthesis. The actions of solvent and of side chains in the positions 2 and 3 on the conformational arrangement of the peptide backbone and the disulfide group were investigated by means of CD spectroscopy. Some mechanisms which co-operate in stabilizing the oxytocin conformation were identified. Hence, it may be deduced, that the amino acid sequence in the positions 1-3 determines the spatial arrangement characteristic for oxytocin, at least in a protonating medium.

Synthesis, and Helix or Hairpin-Turn Secondary Structures of “Mixed” α/β-Peptides Consisting of Residues with Proteinogenic Side Chains and of 2-Amino-2-methylpropanoic Acid (Aib).

ChemInform ◽  
2006 ◽  
Vol 37 (49) ◽  
Author(s):  
Dieter Seebach ◽  
Bernhard Jaun ◽  
Radovan Sebesta ◽  
Raveendra I. Mathad ◽  
Oliver Floegel ◽  
...  
Keyword(s):  
Secondary Structures ◽  
Side Chains
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