scholarly journals Solid-Phase Synthesis of an Insect Pyrokinin Analog Incorporating an Imidazoline Ring as Isosteric Replacement of a trans Peptide Bond

Molecules ◽  
2021 ◽  
Vol 26 (11) ◽  
pp. 3271
Author(s):  
Krzysztof Kaczmarek ◽  
Barbara Pacholczyk-Sienicka ◽  
Łukasz Albrecht ◽  
Janusz Zabrocki ◽  
Ronald J. Nachman
Keyword(s):  
Bioactive Peptides ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Peptide Bond ◽  
Synthetic Method ◽  
Phase Synthesis ◽  
Iminium Salt ◽  
Diaminopropanoic Acid ◽  
Imidazoline Ring ◽  
Ring Motif

A facile solid-phase synthetic method for incorporating the imidazoline ring motif, a surrogate for a trans peptide bond, into bioactive peptides is reported. The example described is the synthesis of an imidazoline peptidomimetic analog of an insect pyrokinin neuropeptide via a cyclization reaction of an iminium salt generated from the preceding amino acid and 2,4-diaminopropanoic acid (Dap).

scholarly journals Solid Phase Synthesis of an Insect Pyrokinin Analog Incorporating an Imidazoline Ring as Isosteric Replacement of a trans Peptide Bond

2021 ◽  
Author(s):  
Krzysztof Kaczmarek ◽  
Barbara Pacholczyk-Sienicka ◽  
Łukasz Albrecht ◽  
Janusz Zabrocki ◽  
Ronald Nachman
Keyword(s):  
Bioactive Peptides ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Peptide Bond ◽  
Synthetic Method ◽  
Phase Synthesis ◽  
Iminium Salt ◽  
Diaminopropanoic Acid ◽  
Imidazoline Ring ◽  
Ring Motif

A facile solid-phase synthetic method for incorporating the imidazoline ring motif, a surrogate for a trans peptide bond, into bioactive peptides is reported. The example described is the synthesis of an imidazoline peptidomimetic analog of an insect pyrokinin neuropeptide via a cyclization reaction of an iminium salt generated from the preceding amino acid and 2,4-diaminopropanoic acid (Dap).

Parallel Solid-Phase Synthesis of Partially Modified Retro and Retro-Inverso ψ[NHCH(CF3)]-Gly Peptides

2002 ◽  
Vol 67 (9) ◽  
pp. 1305-1319 ◽  
Author(s):  
Monica Sani ◽  
Pierfrancesco Bravo ◽  
Alessandro Volonterio ◽  
Matteo Zanda
Keyword(s):  
Amino Acid ◽  
Mild Condition ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Peptide Bond ◽  
Amino Acid Esters ◽  
Phase Synthesis ◽  
Acid Esters

The parallel solid-phase synthesis of small libraries of molecules belonging to a novel class of retro and retro-inverso peptides having a ψ[NHCH(CF3)] surrogate of the conventional retro-peptide bond (NH-CO) has been accomplished. Key step for the synthesis of the -NHCH(CF3)- unit is a Michael-type N-addition of resin bound α-amino acid esters H-AA1-OWang (1), dipeptide H-Val-Gly-OWang (8), and tripeptide H-Val-Val-Ala-OWang (12) to (S)-3-(E-enoyl)-1,3-oxazolidin-2-one (3), which took place very effectively under mild condition. Chemoselective exocyclic oxazolidinone cleavage, followed by parallel couplings of the resulting polymer-bound pseudopeptides WangO-AA1-ψ[NHCH(CF3)]-Gly-OH (5), WangO-Gly-Val-ψ[NHCH(CF3)]-Gly-OH (10), and WangO-Ala-Val-Val-ψ[NHCH(CF3)]-Gly-OH (14) with different α-amino acid esters afforded, after release from the resin, a representative set of ψ[NHCH(CF3)] retro and retro-inverso tripeptides HO-AA1-ψ[NHCH(CF3)]-Gly-AA2-OX1 (7), tetrapeptides HO-Gly-Val-ψ[NHCH(CF3)]-Gly-AA3-OX2 (11), and pentapeptides HO-Ala-Val-Val-ψ[NHCH(CF3)]-Gly-AA4-OX3 (15), respectively, with good to excellent purity in all cases.

scholarly journals The Problem of Aspartimide Formation During Protein Chemical Synthesis Using SEA-Mediated Ligation

2019 ◽  
Author(s):  
Jennifer Bouchenna ◽  
Magalie Sénéchal ◽  
Hervé Drobecq ◽  
Jérôme Vicogne ◽  
Oleg Melnyk
Keyword(s):  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Side Reaction ◽  
Peptide Bond ◽  
Protein Targets ◽  
Chemical Ligation ◽  
Phase Synthesis ◽  
Bond Forming ◽  
Aspartimide Formation ◽  
Peptide Segments

Aspartimide formation often complicates the solid phase synthesis of peptides. Much less discussed is the potential occurrence of this side-reaction during the coupling of peptide segments using chemoselective peptide bond forming reactions such as the native chemical ligation and extended methods. Here we describe how to manage this problem using bis(2-sulfenylethyl)amido (SEA)-mediated ligation and SUMO-2/SUMO-3 as protein targets.<br>

scholarly journals The Pictet-Spengler Reaction Updates Its Habits

Molecules ◽  
2020 ◽  
Vol 25 (2) ◽  
pp. 414 ◽  
Author(s):  
Andrea Calcaterra ◽  
Laura Mangiardi ◽  
Giuliano Delle Monache ◽  
Deborah Quaglio ◽  
Silvia Balducci ◽  
...  
Keyword(s):  
Total Synthesis ◽  
Multicomponent Reaction ◽  
Michael Addition ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Synthetic Method ◽  
Ring Closing Metathesis ◽  
Phase Synthesis ◽  
Acid Catalyzed ◽  
High Yields

The Pictet-Spengler reaction (P-S) is one of the most direct, efficient, and variable synthetic method for the construction of privileged pharmacophores such as tetrahydro-isoquinolines (THIQs), tetrahydro-β-carbolines (THBCs), and polyheterocyclic frameworks. In the lustro (five-year period) following its centenary birthday, the P-S reaction did not exit the stage but it came up again on limelight with new features. This review focuses on the interesting results achieved in this period (2011–2015), analyzing the versatility of this reaction. Classic P-S was reported in the total synthesis of complex alkaloids, in combination with chiral catalysts as well as for the generation of libraries of compounds in medicinal chemistry. The P-S has been used also in tandem reactions, with the sequences including ring closing metathesis, isomerization, Michael addition, and Gold- or Brønsted acid-catalyzed N-acyliminium cyclization. Moreover, the combination of P-S reaction with Ugi multicomponent reaction has been exploited for the construction of highly complex polycyclic architectures in few steps and high yields. The P-S reaction has also been successfully employed in solid-phase synthesis, affording products with different structures, including peptidomimetics, synthetic heterocycles, and natural compounds. Finally, the enzymatic version of P-S has been reported for biosynthesis, biotransformations, and bioconjugations.

scholarly journals The Problem of Aspartimide Formation During Protein Chemical Synthesis Using SEA-Mediated Ligation

2019 ◽  
Author(s):  
Jennifer Bouchenna ◽  
Magalie Sénéchal ◽  
Hervé Drobecq ◽  
Jérôme Vicogne ◽  
Oleg Melnyk
Keyword(s):  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Side Reaction ◽  
Peptide Bond ◽  
Protein Targets ◽  
Chemical Ligation ◽  
Phase Synthesis ◽  
Bond Forming ◽  
Aspartimide Formation ◽  
Peptide Segments

Aspartimide formation often complicates the solid phase synthesis of peptides. Much less discussed is the potential occurrence of this side-reaction during the coupling of peptide segments using chemoselective peptide bond forming reactions such as the native chemical ligation and extended methods. Here we describe how to manage this problem using bis(2-sulfenylethyl)amido (SEA)-mediated ligation and SUMO-2/SUMO-3 as protein targets.<br>

Sign in / Sign up

Export Citation Format

Share Document