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Can I read Structure-based design of thioether-bridged cyclic phosphopeptides binding to Grb2-SH2 domain on EtoBox?
Structure-based design of thioether-bridged cyclic phosphopeptides binding to Grb2-SH2 domain by Peng Li; Megan L Peach; Manchao Zhang; Hongpeng Liu; Dajun Yang; Marc Nicklaus; Peter P Roller is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is Structure-based design of thioether-bridged cyclic phosphopeptides binding to Grb2-SH2 domain about?
A series of phosphotyrosine containing cyclic peptides was designed and synthesized based upon the phage library derived cyclopeptide, G1TE. Considering the type-I beta-turn feature of peptidic ligand binding to Grb2 SH2 domain, we introduce alpha,alpha-disubstituted cyclic amino acid, Ach, into the 4th position of the cyclic peptide to induce a local right handed 3(10) helical conformation. In order to stabilize the favorable binding conformation, the bulky and hydrophobic amino acids, neopentylglycine (NPG) and phenylalanine, were introduced into the 8th and 2nd positions of the peptide ligand, respectively. To facilitate the sidechain of pTyr3 reaching into the phosphotyrosine binding pocket, a less bulky alanine was preferred in position 1. Based upon these global modifications, a highly potent peptide ligand 12 was discovered with an IC(50)=1.68 nM, evaluated by ELISA binding essay. Ligand 12 is at least 10(5) more potent than the lead peptide, termed G1TE.
Who reads Structure-based design of thioether-bridged cyclic phosphopeptides binding to Grb2-SH2 domain?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Peng Li; Megan L Peach; Manchao Zhang; Hongpeng Liu; Dajun Yang; Marc Nicklaus; Peter P Roller
- Publisher
- Elsevier Science; Elsevier ; Elsevier Ltd.; Elsevier BV (ISSN 0960-894X)
- Published
- 2003
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)