60117-24-0Relevant articles and documents
Environmentally friendly SPPS I. Application of NaOH in 2-MeTHF/methanol for Fmoc removal
P?ibylka, Adam,Krchňák, Viktor,Schütznerová, Eva
, p. 775 - 779 (2019)
Focusing on the step-by-step transformation of the traditional solid-phase peptide synthesis (SPPS) into an environmentally friendly process, we herein report the elimination of environmentally hazardous components (piperidine, DMF and DCM) from this technique. We developed a synthetic protocol that employs sodium hydroxide in a 2-MeTHF/MeOH mixture for Fmoc group cleavage and uses 2-MeTHF alone as the coupling solvent. The protocol was developed with the most frequently used PS/DVB-based resin. This synthetic strategy was used to prepare Leu-enkephalin amide, and the results (crude purity 99%, yield 62%) were fully comparable to those achieved with the traditional protocol using piperidine, DMF and DCM.
2-(4-Sulfophenylsulfonyl)ethoxycarbonyl group: A new water-soluble N-protecting group and its application to solid phase peptide synthesis in water
Hojo, Keiko,Maeda, Mitsuko,Kawasaki, Koichi
, p. 9293 - 9295 (2004)
Solid phase peptide synthesis is carried out in organic solvents, creating environmental problems after disposal. To avoid this problem, we aimed to perform solid phase peptide synthesis in water. A new water-soluble N-protecting group, 2-(4-sulfophenylsulfonyl)ethoxycarbonyl (Sps) group, was designed and Sps-amino acids were prepared. To evaluate the utility of this technique, Leu-enkephalin amide was prepared by solid phase synthesis using Sps-amino acids in water.
Core-shell-type resins for solid-phase peptide synthesis: Comparison with gel-type resins in solid-phase photolytic cleavage reaction
Kim, Hanyoung,Jin, Ku Cho,Chung, Woo-Jae,Lee, Yoon-Sik
, p. 3273 - 3276 (2004)
(Graph Presented) Novel core-shell-type resins with a rigid core and amino-functionalized flexible shell were prepared with 2,4,6-trichloro-1,3,5- triazine (CNC) and Jeffamine ED-600 starting from 1% cross-linked aminomethyl (AM) polystyrene resins. All o
The application of anisole in greener solid-phase peptide synthesis protocols – Compatibility with green bases in Fmoc removal and new green binary mixture for coupling
Grepl, Martin,P?ibylka, Adam,Pastorek, Milan,Schütznerová, Eva P?ibylka
supporting information, (2021/09/30)
As a step toward green Fmoc solid-phase peptide synthesis (SPPS), we explored the compatibility of the green bases morpholine, 1,8-diazabicyclo[5.4.0]undec-7-ene (DBU) and NaOH with the green solvent anisole as a replacement for the traditionally used hazardous piperidine in N,N-dimethylformamide (DMF) for the Fmoc removal step. Green Fmoc cleavage protocols were optimized for the Fmoc-Ala-NH-Rink resin model and subsequently verified for other Fmoc-amino acids. Only Gly required a modified NaOH-based protocol with the addition of 5 % water. Furthermore, we evaluated the effects of basic treatment on the notorious aspartimide formation as an undesired side product of SPPS. We also introduced a new green solvent mixture, anisole/dimethyl sulfoxide (DMSO) (4:1) for acylation step, which did not cause racemization. The applicability of these new green protocols was shown during SPPS of the pentapeptides Leu-enkephalin and Aib-enkephalin using polystyrene (PS)-based resins. Additionally, we identified the new sequence-dependent side products that formed after treatment with NaOH in anisole/ethanol (EtOH) (1:1).
Sustainable Peptide Synthesis Enabled by a Transient Protecting Group
Avrutina, Olga,Knauer, Sascha,Koch, Niklas,Kolmar, Harald,Meusinger, Reinhard,Uth, Christina
supporting information, p. 12984 - 12990 (2020/06/01)
The growing interest in synthetic peptides has prompted the development of viable methods for their sustainable production. Currently, large amounts of toxic solvents are required for peptide assembly from protected building blocks, and switching to water as a reaction medium remains a major hurdle in peptide chemistry. We report an aqueous solid-phase peptide synthesis strategy that is based on a water-compatible 2,7-disulfo-9-fluorenylmethoxycarbonyl (Smoc) protecting group. This approach enables peptide assembly under aqueous conditions, real-time monitoring of building block coupling, and efficient postsynthetic purification. The procedure for the synthesis of all natural and several non-natural Smoc-protected amino acids is described, as well as the assembly of 22 peptide sequences and the fundamental issues of SPPS, including the protecting group strategy, coupling and cleavage efficiency, stability under aqueous conditions, and crucial side reactions.
Fully automated peptide radiolabeling from [18F]fluoride
Davis, Ryan A.,Drake, Chris,Ippisch, Robin C.,Moore, Melissa,Sutcliffe, Julie L.
, p. 8638 - 8649 (2019/03/21)
The biological properties of receptor-targeted peptides have made them popular diagnostic imaging and therapeutic agents. Typically, the synthesis of fluorine-18 radiolabeled receptor-targeted peptides for positron emission tomography (PET) imaging is a t
CITU: A Peptide and Decarboxylative Coupling Reagent
Degruyter, Justine N.,Malins, Lara R.,Wimmer, Laurin,Clay, Khalyd J.,Lopez-Ogalla, Javier,Qin, Tian,Cornella, Josep,Liu, Zhiqing,Che, Guanda,Bao, Denghui,Stevens, Jason M.,Qiao, Jennifer X.,Allen, Martin P.,Poss, Michael A.,Baran, Phil S.
supporting information, p. 6196 - 6199 (2017/11/24)
Tetrachloro-N-hydroxyphthalimide tetramethyluronium hexafluorophosphate (CITU) is disclosed as a convenient and economical reagent for both acylation and decarboxylative cross-coupling chemistries. Within the former set of reactions, CITU displays reactiv
Facile synthesis of N-(9-fluorenylmethyloxycarbonyl)-3-amino-3-(4,5- dimethoxy-2-nitrophenyl)propionic acid as a photocleavable linker for solid-phase peptide synthesis
Kim, Jaehi,Kyeong, San,Shin, Dong-Sik,Yeo, Sewon,Yim, Joonhyuk,Lee, Yoon-Sik
, p. 733 - 736 (2013/05/09)
A photocleavable linker, N-(9-fluorenylmethyloxycarbonyl)-3-amino-3-(4,5- dimethoxy-2-nitrophenyl)propionic acid was synthesized from veratraldehyde, with simple reaction and separation steps. This linker was stable under the normal solid-phase peptide sy
Effect of residual water and microwave heating on the half-life of the reagents and reactive intermediates in peptide synthesis
Pernille Tofteng,Pedersen, S?ren L.,Staerk, Dan,Jensen, Knud J.
experimental part, p. 9024 - 9031 (2012/10/18)
Precise microwave heating has changed the way many small molecules are being synthesized and, currently, the field of solid-phase peptide synthesis is undergoing dramatic changes owing to the use of microwave heating. To fully reap the benefits of precise microwave heating for the formation of amide bonds in peptide synthesis, it is important to understand the kinetics of formation and break-down of activated esters and their N-acylation of the nascent peptide chain at elevated temperatures. Herein, we present systematic studies of, first, the rate of formation of activated esters by NMR spectroscopy and, second, their N-acylation during peptide synthesis. A study of the amount of residual water in the solvents revealed a significant effect on electrophilic reagents and intermediates. This observation was expanded into a general study of microwave heating in peptide synthesis.
Benzotriazole-assisted solid-phase assembly of Leu-Enkephalin, amyloid β segment 34-42, and other "difficult" peptide sequences
Katritzky, Alan R.,Haase, Danniebelle N.,Johnsons, Jodie V.,Chung, Alfred
supporting information; experimental part, p. 2028 - 2032 (2009/08/07)
Microwave-assisted solid-phase syntheses of six "difficult" peptides, H-VVSVV-NH2 (3), H-VVVSVV-NH2(4), H-VIVIG-OH (5), H-TVTVTV-NH2 (6), H-VKDGYI-NH2 (7), and H-VKDVYI-NH2 (8), were achieved utilizing N-(Fmoc-α-aminoacyl) benzotriazoles. Extension to the syntheses of Leu-enkephalin (9) and amyloid-β (34-42) (10) demonstrates that this strategy comprises an efficient route to new and known "difficult" peptides.
