364778-12-1Relevant articles and documents
Design strategies for the sequence-based mimicry of side-chain display in protein β-sheets by α/β-peptides
Lengyel, George A.,Horne, W. Seth
supporting information, p. 15906 - 15913,8 (2020/08/24)
The sophistication of folding patterns and functions displayed by unnatural-backbone oligomers has increased tremendously in recent years. Design strategies for the mimicry of tertiary structures seem within reach; however, a general method for the mimicry of sheet segments in the context of a folded protein is an unmet need preventing realization of this goal. Previous work has shown that 1→1 α→β-residue substitutions at cross-strand positions in a hairpin-forming α-peptide sequence can generate an α/β-peptide analogue that folds in aqueous conditions but with a change in side-chain display relative to the natural sequence; this change would prevent application of single β-residue substitutions in a larger protein. Here, we evaluate four different substitution strategies based on replacement of αα dipeptide segments for the ability to retain both sheet folding encoded by a parent α-peptide sequence as well as nativelike side-chain display in the vicinity of the β-residue insertion point. High-resolution structure determination and thermodynamic analysis of folding by multidimensional NMR suggest that three of the four designs examined are applicable to larger proteins.
Design, synthesis, and biological evaluation of novel diarylalkyl amides as TRPV1 antagonists
Li, Fu-Nan,Kim, Nam-Jung,Paek, Seung-Mann,Kwon, Do-Yeon,Min, Kyung Hoon,Jeong, Yeon-Su,Kim, Sun-Young,Park, Young-Ho,Kim, Hee-Doo,Park, Hyeung-Geun,Suh, Young-Ger
experimental part, p. 3557 - 3567 (2009/09/27)
We have developed a new class of diarylalkyl amides as novel TRPV1 antagonists. They exhibited potent 45Ca2+ uptake inhibitions in rat DRG neuron. In particular, the amide 59 was identified as a potent antagonist with IC50 of 57 nM. The synthesis and structure-activity relationship of the diarylalkyl amides are also described.
A mild and selective method for the cleavage of tert-butyl esters
Jackson, Randy W
, p. 5163 - 5165 (2007/10/03)
A method for the cleavage of t-butyl esters using silica gel in refluxing toluene is reported. Good yields of the corresponding carboxylic acids are obtained, and the reaction is selective for t-butyl esters over t-butyl ethers and trimethylsilylethyl (TMSE) esters.
Use of 1,2,3-trisubstituted cyclopropanes as conformationally constrained peptide mimics in SH2 antagonists
Davidson,Martin
, p. 9459 - 9464 (2007/10/03)
Novel conformationally constrained phosphotyrosine pseudopeptide derivatives of the tetrapeptide pY-E-E-I were prepared and evaluated as SH2 binding antagonists. (C) 2000 Elsevier Science Ltd.
