102747-84-2Relevant articles and documents
Probing the role of backbone hydrogen bonds in protein-peptide interactions by amide-to-ester mutations
Eildal, Jonas N. N.,Hultqvist, Greta,Balle, Thomas,Stuhr-Hansen, Nicolai,Padrah, Shahrokh,Gianni, Stefano,Stromgaard, Kristian,Jemth, Per
, p. 12998 - 13007 (2013)
One of the most frequent protein-protein interaction modules in mammalian cells is the postsynaptic density 95/discs large/zonula occludens 1 (PDZ) domain, involved in scaffolding and signaling and emerging as an important drug target for several diseases
Mild oxidative cleavage of 9-BBN-protected amino acid derivatives
Ankner, Tobias,Norberg, Thomas,Kihlberg, Jan
, p. 3767 - 3770 (2015/06/16)
Protection of the amino acid moiety using 9-BBN is an effective method to enable side chain manipulations in synthesis of complex amino acids. We investigated the standard, mild method for deprotection of the 9-BBN group in methanolic chloroform, and found that it relies on a slow oxidation mediated by molecular oxygen. Building on this insight, we have developed a method that allows for a fast and selective deprotection using simple peroxy acid reagents. After Fmoc protection, products were isolated in >90% yield for a series of amino acid derivatives, including a galactosylated derivative of hydroxylysine. A representative set of 9-BBN-protected amino acid derivatives were efficiently deprotected using peracid reagents in excellent yields. Deprotection is orthogonal with several common protecting groups. Its tolerance of highly acid sensitive groups, such as trityl-protected amides and glycosidic linkages, is especially notable.
Protection of carboxamide functions by the trityl residue. Application to peptide synthesis
Sieber,Riniker
, p. 739 - 742 (2007/10/02)
Carboxamide functions may be tritylated by an acid-catalyzed reaction with triphenylmethanol and acetic anhydride in glacial acetic acid. The ω-trityl group of asparagine and glutamine is cleavable by TFA, but stable to strong mineral acids in aqueous solution, as well as to nucleophiles and bases. In peptide syntheses, it is ideally suited for combination with side-chain protections of the t.butyl-type.