24935-97-5

Usage

InChI:InChI=1/C5H9NO3/c1-2-3-9-5(8)6-4-7/h2,7H,1,3-4H2,(H,6,8)

Upstream product

• 50-00-0 formaldehyd 
• 2114-11-6 allyl carbamate 

Downstream Products

• 160978-29-0 N-benzylthiomethyl-carbamic acid allyl ester 
• 1266239-61-5 C₂₆H₂₈N₂O₇S 
• 1266239-60-4 C₂₆H₂₇BrN₂O₇S 
• 4431-79-2 bis(benzylthio)methane 
• 160978-33-6 N^α-tert-butoxycarbonyl-S-allyloxycarbonylaminomethyl-L-cysteine benzylamide 

Relevant academic research and scientific papers

Direct palladium-mediated on-resin disulfide formation from Allocam protected peptides

The synthesis of disulfide-containing polypeptides represents a long-standing challenge in peptide chemistry, and broadly applicable methods for the construction of disulfides are in constant demand. Few strategies exist for on-resin formation of disulfides directly from their protected counterparts. We present herein a novel strategy for the on-resin construction of disulfides directly from Allocam-protected cysteines. Our palladium-mediated approach is mild and uses readily available reagents, requiring no special equipment. No reduced peptide intermediates or S-allylated products are observed, and no residual palladium can be detected in the final products. The utility of this method is demonstrated through the synthesis of the C-carboxy analog of oxytocin.

Modifications of the C6-substituent of penicillin sulfones with the goal of improving inhibitor recognition and efficacy

In order to evaluate the importance of a hydrogen-bond donating substituent in the design of β-lactamase inhibitors, a series of C6-substituted penicillin sulfones, lacking a C2′ substituent, and having an sp 3 hybridized C6, was prepared and evaluated against a representative classes A and C β-lactamases. It was found that a C6 hydrogen-bond donor is necessary for good inhibitory activity, but that this feature alone is not sufficient in this series of C6β-substituted penicillin sulfones. Other factors which may impact the potency of the inhibitor include the steric bulk of the C6 substituent (e.g., methicillin sulfone) which may hinder recognition in the class A β-lactamases, and also high similarity to the natural substrates (e.g., penicillin G sulfone) which may render the prospective inhibitor a good substrate of both classes of enzyme. The best inhibitors had non-directional hydrogen-bonding substituents, such as hydroxymethyl, which may allow sufficient conformational flexibility of the acyl-enzyme for abstraction of the C6 proton by E166 (class A), thus promoting isomerization to the β-aminoacrylate as a stabilized acyl-enzyme.

Allylic protection of thiols and cysteine: I: The allyloxycarbonylaminomethyl group

S-allyloxycarbonylaminomethyl derivatives of thiols in general and cysteine in particular are readily deprotected by palladium catalysed hydrostannolysis with tributyltin hydride in the presence of acetic acid. They are perfectly stable in the basic conditions (piperidine/DMF) of Fmoc group removal but tend to decompose, albeit slowly, in the acidic conditions (TFA/CH2Cl2) of t-Bu and Boc groups removal.