title: Examination of acylated 4-aminopiperidine-4-carboxylic acid residues in the phosphotyrosyl+1 position of Grb2 SH2 domain-binding tripeptides.
abstract: A 4-aminopiperidine-4-carboxylic acid residue was placed in the pTyr+1 position of a Grb2 SH2 domain-binding peptide to form a general platform, which was then acylated with a variety of groups to yield a library of compounds designed to explore potential binding interactions, with protein features lying below the betaD strand. The highest affinities were obtained using phenylethyl carbamate and phenylbutyrylamide functionalities.
authors: Laboratory of Medicinal Chemistry, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, Maryland 21702-1201, USA.
authors: Sang-Uk
authors: SU
authors: Kang
authors: Won Jun
authors: WJ
authors: Choi
authors: Shinya
authors: S
authors: Oishi
authors: Kyeong
authors: K
authors: Lee
authors: Rajeshri G
authors: RG
authors: Karki
authors: Karen M
authors: KM
authors: Worthy
authors: Lakshman K
authors: LK
authors: Bindu
authors: Marc C
authors: MC
authors: Nicklaus
authors: Robert J
authors: RJ
authors: Fisher
authors: Terrence R
authors: TR
authors: Burke
mesh_terms: D000215:Acylation; D001665:Binding Sites; D051380:GRB2 Adaptor Protein / Q000737:chemistry*; D008958:Models, Molecular; D008968:Molecular Conformation; D009842:Oligopeptides / Q000737:chemistry*; D019000:Phosphotyrosine / Q000737:chemistry*; D010880:Piperidines / Q000138:chemical synthesis* / Q000737:chemistry; D018909:src Homology Domains
chemical_list: D051380:GRB2 Adaptor Protein; D009842:Oligopeptides; D010880:Piperidines; D019000:Phosphotyrosine