4353-32-6Relevant articles and documents
Facile synthesis of α-hydroxy carboxylic acids from the corresponding α-amino acids
Stuhr-Hansen, Nicolai,Padrah, Shahrokh,Str?mgaard, Kristian
supporting information, p. 4149 - 4151 (2015/02/02)
An effective and improved procedure is developed for the synthesis of α-hydroxy carboxylic acids by treatment of the corresponding protonated α-amino acid with tert-butyl nitrite in 1,4-dioxane-water. The amino moiety must be protonated and located α to a carboxylic acid function in order to undergo initial diazotization and successive hydroxylation, since neither β-amino acids nor acid derivatives such as esters and amides undergo hydroxylations. The method is successfully applied for the synthesis of 18 proteinogenic amino acids.
A mild Boc deprotection and the importance of a free carboxylate
Thaqi, Ali,McCluskey, Adam,Scott, Janet L.
supporting information; experimental part, p. 6962 - 6964 (2009/04/07)
We report a facile and rapid removal of Boc protecting groups using microwave heating in H2O, with deprotection only requiring a free carboxylic acid group in the starting material. Unlike previous approaches, no additional reagents are required.
The discovery, characterization and crystallographically determined binding mode of an FMOC-containing inhibitor of HIV-1 protease
Rutenber, Earl E.,De Voss, James J.,Hoffman, Lucas,Stroud, Robert M.,Lee, Kwan H.,Alvarez, Juan,McPhee, Fiona,Craik, Charles,Ortiz De Montellano, Paul R.
, p. 1311 - 1320 (2007/10/03)
A pharmacophore derived from the structure of the dithiolane derivative of haloperidol bound in the active site of the HIV-1 protease (HIV-1 PR) has been used to search a three-dimensional database for new inhibitory frameworks. This search identified an FMOC-protected N-tosyl arginine as a lead candidate. A derivative in which the arginine carboxyl has been converted to an amide has been crystallized with HIV-1 PR and the structure has been determined to a resolution of 2.5 A with a final R-factor of 18.5%. The inhibitor binds in an extended conformation that results in occupancy of the S2, S1', and S3' subsites of the active site. Initial structure-activity studies indicate that: (1) the FMOC fluorenyl moiety interacts closely with active site residues and is important for binding; (2) the N(G)-tosyl group is necessary to suppress protonation of the arginine guanidinyl terminus; and (3) the arginine carboxamide function is involved in interactions with the water coordinated to the catalytic aspartyl groups. FMOC-protected arginine derivatives, which appear to be relatively specific and nontoxic, offer promise for the development of useful HIV-1 protease inhibitors.
