6206-42-4Relevant academic research and scientific papers
Continuous synthesis of a tripeptide by successive condensation and transesterification catalyzed by two immobilized proteinases in organic solvent.
Kimura,Yoshida,Muraya,Nakanishi,Matsuno
, p. 1433 - 1440 (1990)
The tripeptide Z-GlyPheLeuNH2 was continuously synthesized in a high yield from three amino acid derivatives, Z-Gly, PheOMe, and LeuNH2, by immobilized thermolysin (IMT) and immobilized alpha-chymotrypsin (IMC) in an organic solvent, ethyl acetate. The op
Phosphorus pentoxide for amide and peptide bond formation with minimal by-products
Erapalapati, Venkataramana,Hale, Umatai A.,Madhavan, Nandita
supporting information, (2019/11/21)
Phosphorus pentoxide and DMAP are used for amide bond formation from carboxylic acids and amines. Dipeptides and amides have been synthesized using this reagent in 42–77% yields and >99% ees. The protocol is attractive as it occurs at ambient temperature, the formation of organic by-products is minimal and the reagent can be readily quenched using water. Furthermore, excellent enantioselectivities are observed without the use of harsh triazole based additives.
Pd-Catalyzed Site-Selective C(sp2)-H Olefination and Alkynylation of Phenylalanine Residues in Peptides
Zheng, Yong,Song, Weibin
supporting information, (2019/05/08)
Pd-catalyzed site-selective C(sp2)-H olefination and alkynylation of phenylalanine residues in peptides are described. The amino acids within the peptides are used as native bidentate directing groups to facilitate C-H functionalization. This p
Postsynthetic Modification of Phenylalanine Containing Peptides by C-H Functionalization
Terrey, Myles J.,Perry, Carole C.,Cross, Warren B.
, p. 104 - 108 (2019/01/11)
New methods for peptide modification are in high demand in drug discovery, chemical biology, and materials chemistry; methods that modify natural peptides are particularly attractive. A Pd-catalyzed, C-H functionalization protocol for the olefination of phenylalanine residues in peptides is reported, which is compatible with common amino acid protecting groups, and the scope of the styrene reaction partner is broad. Bidentate coordination of the peptide to the catalyst appears crucial for the success of the reaction.
Pd-catalyzed intramolecular C(sp2)-H amination of phenylalanine moieties in dipeptides: Synthesis of indoline-2-carboxylate-containing dipeptides
Zheng, Yong,Song, Weibin,Zhu, Yefu,Wei, Bole,Xuan, Lijiang
supporting information, p. 2402 - 2405 (2018/04/12)
A palladium-catalyzed intramolecular C(sp2)-H amination of phenylalanine moieties in dipeptides is described. By this protocol, a series of indoline-2-carboxylate-containing dipeptides were synthesized from dipeptides. The N-protected amino aci
Direct Hydroxylation of Benzene to Phenol by Cytochrome P450BM3 Triggered by Amino Acid Derivatives
Shoji, Osami,Yanagisawa, Sota,Stanfield, Joshua Kyle,Suzuki, Kazuto,Cong, Zhiqi,Sugimoto, Hiroshi,Shiro, Yoshitsugu,Watanabe, Yoshihito
supporting information, p. 10324 - 10329 (2017/08/22)
The selective hydroxylation of benzene to phenol, without the formation of side products resulting from overoxidation, is catalyzed by cytochrome P450BM3 with the assistance of amino acid derivatives as decoy molecules. The catalytic turnover rate and the total turnover number reached 259 min?1 P450BM3?1 and 40 200 P450BM3?1 when N-heptyl-l-proline modified with l-phenylalanine (C7-l-Pro-l-Phe) was used as the decoy molecule. This work shows that amino acid derivatives with a totally different structure from fatty acids can be used as decoy molecules for aromatic hydroxylation by wild-type P450BM3. This method for non-native substrate hydroxylation by wild-type P450BM3 has the potential to expand the utility of P450BM3 for biotransformations.
One-step C-terminal deprotection and activation of peptides with peptide amidase from stenotrophomonas maltophilia in neat organic solvent
Arif, Muhammad I.,Toplak, Ana,Szymanski, Wiktor,Feringa, Ben L.,Nuijens, Timo,Quaedflieg, Peter J. L. M.,Wu, Bian,Janssen, Dick B.
, p. 2197 - 2202 (2014/07/21)
Chemoenzymatic peptide synthesis is a rapidly developing technology for cost effective peptide production on a large scale. As an alternative to the traditional C→N strategy, which employs expensive N-protected building blocks in each step, we have investigated an N→C extension route that is based on activation of a peptide C-terminal amide protecting group to the corresponding methyl ester. We found that this conversion is efficiently catalysed by Stenotrophomonas maltophilia peptide amidase in neat organic media. The system excludes the possibility of internal peptide cleavage as the enzyme lacks intrinsic protease activity. The produced peptide methyl ester was used for peptide chain extension in a kinetically controlled reaction by a thermostable protease.
Processes for forming amide bonds and compositions related thereto
-
Page/Page column 29; 30, (2015/01/07)
The disclosure relates to methods for producing amide bonds and reagents related thereto. In some embodiments, the disclosure relates to methods of producing an amide comprising mixing an O-silylated thionoester and an amine under conditions such that an amide is formed. In another embodiment, the disclosure relates to mixing a thiolacid, a silylating agent, and an amine under conditions such that an amide is formed.
Facile amide formation via S -nitrosothioacids
Pan, Jia,Devarie-Baez, Nelmi O.,Xian, Ming
supporting information; experimental part, p. 1092 - 1094 (2011/04/25)
Here we report a novel amide bond formation strategy from simple thioacid and amine starting materials. The reaction is mediated by unstable but very reactive S-nitrosothioacid intermediates. This fast reaction under mild conditions should be useful in synthesis.(Figure Presented)
In situ carboxyl activation using a silatropic switch: A new approach to amide and peptide constructions
Wu, Wenting,Zhang, Zhihui,Liebeskind, Lanny S.
, p. 14256 - 14259 (2011/11/05)
The novel reactivity of O-silylthionoesters with amine nucleophiles to generate oxoamides (rather than thioamides) is described. A straightforward first-generation trimethylsilylation protocol using bistrimethylsilylacetamide (BSA) combined with the unique reactivity of the O-silylthionoesters toward 1° and 2° amines to generate oxoamides provides the simplest means of activating a thiol acid for peptide bond formation at neutral pH. Excellent stereoretention is observed.
