5874-76-0

Upstream product

• 2788-84-3 (S)-serine methyl ester 
• 1145-80-8 N-(benzyloxycarbonyl)-L-serine 
• 5249-65-0 N-carbobenzoxy-L-serine-2,4-dinitrophenol 
• 5680-80-8 methyl (2S)-2-amino-3-hydroxypropanoate hydrochloride 

Downstream Products

• 2768-54-9 Z-Ser-Ser-OH 
• 6620-95-7 L-seryl-L-serine 
• 126886-85-9 Z-Ala-Ser-Ser-OMe 
• 131458-44-1 benzyl (carbamoylcarbonyl)carbamate 
• 22839-30-1 Z-Ser-Ser-NH₂ 
• 84765-47-9 Z-L-Ser(OH)-ΔAla-OMe 
• 131458-43-0 Z-NH-CO-CO-NH-CO-CO₂Me 
• 2488-23-5 N-(N-Benzyloxycarbonyl-L-seryl)-L-serin-hydrazid 

Relevant academic research and scientific papers

Protein backbone modification by novel C(α)-C side-chain scission

α-Ketoamide (-NH-CO-CO-) units in intact peptides are generated from Ser/Thr residues via Ru(VIII)-catalyzed C(α)-C side-chain scission. Facets associated with this novel α-carbon modification have been probed with 75 peptides chosen to represent every possible peptide environment. The reactions were carried out at room temperature with in situ generated Ru(VIII) in biphasic (CH3CN/CCl4/pH 3 phosphate buffer, 1:1:2 v/v) medium. Whereas Ser/Thr residues placed at the C-terminal end in peptides undergo N-C bond scission leading to des-Ser/Thr peptide amides - thus acting as Gly equivalents in simulating the α-amidating action of pituitary enzymes - those located at the N-terminal or nonterminal or even at the C-terminal position (protected as amide) were found to undergo oxidative C-C bond scission (involving C(α) and C side-chain bond), resulting in the generation of α-ketoamide (-NH-CO-CO-) units in the intact peptide backbone. The difference in the products arising from C(α)-C side-chain scission of Ser/Thr esters and amides is rationalized on the basis of a common mechanism involving either oxaloesters [PeP-NH-CO-COX; X = OMe] or oxalamides [X = NH2 or NH-Pep] arising from the oxidation of initially formed carbinolamide intermediates [Pep-NH-CH(OH)-COX], wherein, while the former are shown to undergo hydrolysis to terminal amides [Pep-NH2], the oxalamides are found to be stable to hydrolysis. Ancillary noteworthy findings are those of peptide bond scission when contiguous Ser-Ser/Thr-Thr residues are present and the oxidative cleavage at C-terminal Tyr/Trp sites generating des amides. The oxidative methodology presented here is mild, simple, and practical and proceeds with chiral retention. The insensitivity of a large number of amino acid residues, such as Gly, Ala, Leu, Asn, Gln, Asp, Glu, Pro, Arg, Phe, Lys, Val, and Aib, and N-protecting groups, such as Boc, Z, and Bz, toward Ru(VIII) under the experimental conditions should make this methodology practical and useful. Sulfur-containing amino acids Cys and Met get oxidized to sulfones in the products.

Human interferon-related peptides, antigens, antibodies and process for preparing the same

Human interferons related peptides and derivatives thereof, antigens, antibodies prepared therefrom, immobilized antibodies to be used for affinity chromatography, and novel method for assaying human interferons by using said affinity chromatography.