scholarly journals The role ofEscherichia coliribosomal proteins L7 and L12 in peptide chain propagation

FEBS Letters ◽  
1977 ◽  
Vol 73 (1) ◽  
pp. 1-5 ◽  
Keyword(s):  
Chain Propagation ◽  
Peptide Chain

scholarly journals Chemoenzymatic synthesis of polypeptides in neat 1,1,1,2-tetrafluoroethane solvent

RSC Advances ◽  
2018 ◽  
Vol 8 (63) ◽  
pp. 35936-35945 ◽  
Author(s):  
Isabel S. Aguirre-Díaz ◽  
Carmina Montiel ◽  
Ismael Bustos-Jaimes ◽  
Yaocihuatl Medina-Gonzalez ◽  
Alberto Tecante ◽  
...  
Keyword(s):  
Chain Propagation ◽  
Chemoenzymatic Synthesis ◽  
Peptide Chain ◽  
Polypeptide Synthesis ◽  
Reverse Hydrolysis ◽  
Hydrolysis Reactions

Chemoenzymatic polypeptide synthesis offers several advantages over chemical or other biological routes, however, the use of aqueous-based media suffers from reverse hydrolysis reactions that challenge peptide chain propagation.

Sulfamides Direct Radical-Mediated Chlorination of Aliphatic C–H Bonds

2019 ◽  
Author(s):  
Melanie Short ◽  
Mina Shehata ◽  
Matthew Sanders ◽  
Jennifer Roizen
Keyword(s):  
Hydrogen Atom ◽  
Transfer Reaction ◽  
Hydrogen Atom Transfer ◽  
Chain Propagation ◽  
Propagation Mechanism ◽  
Atom Transfer ◽  
Radical Chain ◽  
Radical Intermediates ◽  
Transfer Processes ◽  
Unusual Position

Sulfamides guide intermolecular chlorine transfer to gamma-C(sp<sup>3</sup>) centers. This unusual position-selectivity arises because accessed sulfamidyl radical intermediates engage in otherwise rare 1,6-hydrogen-atom transfer processes. The disclosed chlorine-transfer reaction relies on a light-initiated radical chain-propagation mechanism to oxidize C(sp<sup>3</sup>)-H bonds.

Sulfamides Direct Radical-Mediated Chlorination of Aliphatic C–H Bonds

2019 ◽  
Author(s):  
Melanie Short ◽  
Mina Shehata ◽  
Matthew Sanders ◽  
Jennifer Roizen
Keyword(s):  
Hydrogen Atom ◽  
Transfer Reaction ◽  
Hydrogen Atom Transfer ◽  
Chain Propagation ◽  
Propagation Mechanism ◽  
Atom Transfer ◽  
Radical Chain ◽  
Radical Intermediates ◽  
Transfer Processes ◽  
Unusual Position

Sulfamides guide intermolecular chlorine transfer to gamma-C(sp<sup>3</sup>) centers. This unusual position-selectivity arises because accessed sulfamidyl radical intermediates engage in otherwise rare 1,6-hydrogen-atom transfer processes. The disclosed chlorine-transfer reaction relies on a light-initiated radical chain-propagation mechanism to oxidize C(sp<sup>3</sup>)-H bonds.

Cholecystokinin Heptapeptide Analogues with Multiple Modification in Peptide Chain

1993 ◽  
Vol 58 (11) ◽  
pp. 2761-2765 ◽  
Author(s):  
Jan Hlaváček ◽  
Jana Pírková ◽  
Miroslava Žertová ◽  
Jan Pospíšek ◽  
Lenka Maletínská ◽  
...  
Keyword(s):  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Peptide Chain ◽  
Phase Synthesis ◽  
C Terminus

Using solid phase synthesis we prepared the cholecystokinin fragment Boc-CCK-7 (Boc-Tyr(SO3-Na+)-Met-Gly-Trp-Met-Asp-Phe-NH2) Ia and its seven analogues Ib - Ih. In the analogues Ib and Ic the Met residue in the carboxyterminal part of the molecule was substituted for L- or D-Phe Me3. In the analogues Id and Ie with Phe residue substituted by L- or D-Phe Me3 the Neo was inserted in the place of this Met residue and in the analogues If and Ig, an addition to PheMe3 substitution in the carboxyterminus, both Met residues were replaced for Neo. This dual substitution for Met residues was also applied in the analogue Ih with coded Phe residue in the C-terminus.

Fmoc Solid Phase Peptide Synthesis

1999 ◽  
Keyword(s):  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Peptide Chain ◽  
Standard Approach ◽  
Side Chain ◽  
Complex Structures ◽  
Protein Conjugation ◽  
Chemoselective Ligation ◽  
Routine Production

In the years since the publication of Atherton and Sheppard's volume, the technique of Fmoc solid-phase peptide synthesis has matured considerably and is now the standard approach for the routine production of peptides. The basic problems outstanding at the time of publication of this earlier work have now been, for the most part, solved. As a result, innovators in the field have focussed their efforts to develop methodologies and chemistry for the synthesis of more complex structures. The focus of this new volume is much broader, and covers not only the essential procedures for the production of linear peptides but also more advanced techniques for preparing cyclic, side-chain modified, phospho- and glycopeptides. Many other methods also deserving attention have been included: convergent peptide synthesis; peptide-protein conjugation; chemoselective ligation; and chemoselective purification. The difficult preparation of cysteine and methionine-containing peptides is also covered, as well as methods for overcoming aggregation during peptide chain assembly and a survey of available automated instrumentation.

scholarly journals Small and Simple, yet Sturdy: Conformationally Constrained Peptides with Remarkable Properties

2021 ◽  
Vol 22 (4) ◽  
pp. 1611
Author(s):  
Krištof Bozovičar ◽  
Tomaž Bratkovič
Keyword(s):  
Chemical Space ◽  
Structure Optimization ◽  
Peptide Chain ◽  
Conformationally Constrained ◽  
Drug Candidates ◽  
Conformational Constraints ◽  
Macrocyclic Peptides ◽  
Constrained Peptides ◽  
Sheer Size

The sheer size and vast chemical space (i.e., diverse repertoire and spatial distribution of functional groups) underlie peptides’ ability to engage in specific interactions with targets of various structures. However, the inherent flexibility of the peptide chain negatively affects binding affinity and metabolic stability, thereby severely limiting the use of peptides as medicines. Imposing conformational constraints to the peptide chain offers to solve these problems but typically requires laborious structure optimization. Alternatively, libraries of constrained peptides with randomized modules can be screened for specific functions. Here, we present the properties of conformationally constrained peptides and review rigidification chemistries/strategies, as well as synthetic and enzymatic methods of producing macrocyclic peptides. Furthermore, we discuss the in vitro molecular evolution methods for the development of constrained peptides with pre-defined functions. Finally, we briefly present applications of selected constrained peptides to illustrate their exceptional properties as drug candidates, molecular recognition probes, and minimalist catalysts.

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