195258-67-4Relevant articles and documents
Late Stage Phosphotyrosine Mimetic Functionalization of Peptides Employing Metallaphotoredox Catalysis
Brzozowski, Martin,Chen, Hao,Mao, Runyu,Nguyen, Nghi H.,Sleebs, Brad E.
supporting information, p. 4244 - 4249 (2021/06/28)
Access to phosphotyrosine (pTyr) mimetics requires multistep syntheses, and therefore late stage incorporation of these mimetics into peptides is not feasible. Here, we develop and employ metallaphotoredox catalysis using 4-halogenated phenylalanine to afford a variety of protected pTyr mimetics in one step. This methodology was shown to be tolerant of common protecting groups and applicable to the late stage pTyr mimetic modification of protected and unprotected peptides, and peptides of biological relevance.
An Intrinsic Hydrophobicity Scale for Amino Acids and Its Application to Fluorinated Compounds
Hoffmann, Waldemar,Langenhan, Jennifer,Huhmann, Susanne,Moschner, Johann,Chang, Rayoon,Accorsi, Matteo,Seo, Jongcheol,Rademann, J?rg,Meijer, Gerard,Koksch, Beate,Bowers, Michael T.,von Helden, Gert,Pagel, Kevin
supporting information, p. 8216 - 8220 (2019/05/21)
More than 100 hydrophobicity scales have been introduced, with each being based on a distinct condensed-phase approach. However, a comparison of the hydrophobicity values gained from different techniques, and their relative ranking, is not straightforward
Synthesis and binding studies of two new macrocyclic receptors for the stereoselective recognition of dipeptides
Castilla, Ana Maria,Ballester, Pablo,Conn, M. Morgan
supporting information; experimental part, (2010/07/18)
We present here the design, synthesis, and analysis of a series of receptors for peptide ligands inspired by the hydrogen-bonding pattern of protein β-sheets. The receptors themselves can be regarded as strands 1 and 3 of a three-stranded β-sheet, with crosslinking between the chains through the 4-position of adjacent phenylalanine residues. We also report on the conformational equilibria of these receptors in solution as well as on their tendency to dimerize. 1H NMR titration experiments are used to quantify the dimerization constants, as well as the association constant values of the 1:1 complexes formed between the receptors and a series of diamides and dipeptides. The receptors show moderate levels of selectivity in the molecular recognition of the hydrogen-bonding pattern present in the diamide series, selecting the α-amino acid-related hydrogen-bonding functionality. Only one of the two cyclic receptors shows modest signs of enantioselectivity and moderate diastereoselectivity in the recognition of the enantiomers and diastereoisomers of the Ala-Ala dipeptide (DDG0 1 (DD-DL) = -1.08 kcal/mol and DDG0 1(DD-LD) = -0.89 kcal/mol). Surprisingly, the linear synthetic precursors show higher levels of stereoselectivity than their cyclic counterparts.