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"Nα,Nε-bis(trifluoroacetyl)-L-lysine" is a chemical compound derived from the amino acid L-lysine. In Nα,Nε-bis(trifluoroacetyl)-L-lysine, the α-amino group (Nα) and the ε-amino group (Nε) of L-lysine are each acylated with a trifluoroacetyl group. Trifluoroacetyl is a highly electronegative acyl group, which can significantly alter the reactivity and properties of the lysine residue. This modification is often used in peptide synthesis to protect the amino groups from unwanted side reactions, ensuring that they remain available for subsequent coupling steps in the synthesis of larger peptide structures. The compound is a white crystalline solid and is soluble in organic solvents. It is used as a protecting group in peptide chemistry, allowing for the controlled synthesis of complex peptide sequences.

329-53-3

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329-53-3 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 329-53-3 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 3,2 and 9 respectively; the second part has 2 digits, 5 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 329-53:
(5*3)+(4*2)+(3*9)+(2*5)+(1*3)=63
63 % 10 = 3
So 329-53-3 is a valid CAS Registry Number.

329-53-3Relevant academic research and scientific papers

N-trifluoroacyl lysine derivatives in the synthesis of L-lysyl-L-glutamic acid

Cherevin,Gulevich,Popova,Zubreichuk,Knizhnikov

, p. 1427 - 1431 (2008/09/16)

Conditions were developed for simultaneous preparation of N a-trifluoroacetyl-L-lysine and N α,N a-bis(trifluoroacetyl)-L-lysine at overall conversion of initial lysine monohydrochloride up to 82%. By reaction of dimethyl L-glutamate with N α,N a-bis(trifluoroacetyl)-L-lysyl chloride in the presence of triethylamine or with N α- carboxyanhydride of N a-trifluoroacetyl-L-lysine with subsequent removing protecting groups in the formed dipeptides by treating with water-ethanol solution of sodium hydroxide we obtained L-lysyl-L-glutamic acid. Physicochemical characteristics of samples obtained coincided with characteristics of L-lysyl-L-glutamic acid described in the literature thus suggesting that no racemization occurred either at the stage of peptide bond formation or at deprotection.

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