Peptides are prime drug candidates due to their high specificity of action but are disadvantaged by low proteolytic stability. Here, we focus on the development of stabilized analogues of EPI-X4, an endogenous peptide antagonist of CXCR4. We synthesized macromolecular peptide conjugates and performed side-by-side comparison with their albumin-binding counterparts and considered monovalent conjugates, divalent telechelic conjugates, and Y-shaped peptide dimers. All constructs were tested for competition with the CXCR4 antibody−receptor engagement, inhibition of receptor activation, and inhibition of the CXCR4tropic human immunodeficiency virus infection. We found that the Y-shaped conjugates were more potent than the parent peptide and at the same time more stable in human plasma, with a favorable outlook for translational studies.

Gas-phase action and fluorescence spectroscopy of fluorescein anions and two derivatives reveal important information on what determines the Stokes shift.

A high-yielding palladium-catalyzed C–S cross-coupling is presented for utilization in carbohydrate chemistry as a key transformation for attachment of a second chelating sulfur atom that allows the exploitation of a latent–active glycosylation strategy with Cu­(OTf)2 as the promoter. The novel approach employs o-Br-benzyl thioglycosides as latent glycosyl donors and o-SMe-benzyl thioglycosides as the active counterparts.