Selective N-terminal functionalization of native peptides and proteins.

Selective N-terminal functionalization of native peptides and proteins† †Electronic supplementary information (ESI) available: Experimental details. See DOI: 10.1039/c6sc04744k Click here for additional data file.

Designing a new tetrapeptide to inhibit the BIR3 domain of the XIAP protein via molecular dynamics simulations

The XIAP protein is a member of apoptosis proteins family. The XIAP protein plays a central role in the inhibition of apoptosis and consists of three Baculoviral IAP Repeat domains. The BIR3 domain binds directly to the N-terminal of caspase-9 and therefore it inhibits apoptosis. N-terminal tetrapeptide region of SMAC protein can bind to BIR3, inhibit it and subsequently induce apoptosis. In th...

Decarboxylative alkylation for site-selective bioconjugation of native proteins via oxidation potentials.

The advent of antibody-drug conjugates as pharmaceuticals has fuelled a need for reliable methods of site-selective protein modification that furnish homogeneous adducts. Although bioorthogonal methods that use engineered amino acids often provide an elegant solution to the question of selective functionalization, achieving homogeneity using native amino acids remains a challenge. Here, we expl...

Indium mediated allylation in peptide and protein functionalization.

Indium-mediated allylation has been used in the site-selective functionalization of N-terminal aldehydes of peptides and proteins. This is the first demonstration of indium-mediated C-C bond formation in protein labelling studies under mild and environmentally friendly conditions.

Cysteine Promoted C-Terminal Hydrazinolysis of Native Peptides and Proteins**

Tagging the terminus: N→S acyl transfer in native peptides and proteins can be reliably intercepted with hydrazine. The method allows selective labeling and ligation, without recourse to the use of protein-splicing elements. NCL=native chemical ligation.