123253-91-8

Upstream product

• 15761-38-3 L-N-Boc-Ala 
• 68858-20-8 Fmoc-Val-OH 
• 35661-60-0 Fmoc-Leu-OH 
• 150009-58-8 9-fluorenylmethoxycarbonyl-O-benzyl-L-aspartic acid 
• 13734-41-3 t-Boc-L-valine 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 13574-13-5 Boc-Glu(OBzl)-OH 

Relevant academic research and scientific papers

Photo-triggered selective C-terminal N-methylamidative cleavage of polyethyleneglycol-bound peptides

A novel liquid-phase method has been designed for the photolytic release of the attached peptides, directly as their C-terminal N-methylamides, under mild conditions in excellent yields and purity. The present approach provides fully side-chain protected peptide N-methylamides, useful for segment condensation and facilitate photocontrolled release of biologically active peptides for therapeutic applications.

Polymer-supported Solid-phase Synthesis of C-Terminal Peptide N-Methylamides Using a Modified Photoremovable 3-Nitro-4-N-methylaminomethylpolystyrene Support

Cross-linked polystyrene resin containing 3-nitro-4-N-methylaminomethyl function has been prepared from Merrifield's chloromethylated polystyrene by a two-step polymer-analogous reaction and developed as a modified photoremovable polymeric support in the solid-phase synthesis of C-terminal N-methyl peptide-amides.This support has been investigated for its use in the solid-phase synthesis of C-terminal N-methyl peptides amides.As model reactions, aliphatic and aromatic carboxylic acids and Boc-amino acids have been coupled with the modified resin and cleaved in the form of N-methyl substituted amides on photolysis at 350 nm under neutral conditions at room temperature.The modified support is found to be stable under the usual conditions of activation, coupling and deprotection of functional groups in solid-phase peptide synthesis.The application of the modified resin is illustrated by the solid-phase synthesis of Boc-Asn-Gly-NHMe.Boc-Leu-Ala-Val-NHMe and Boc-Ala-Asp(OBz)-Leu-Ala-Val-NHMe in 55-65percent overall yield.The present methode avoids the rigorous conditions of basic and acidic cleavages as well as the direct interaction of methylamine with the C-terminal residue of the peptides for its conversion to N-methyl amide form.