title: The aqueous conformation of cyclo(1,6)Ac-Cys-Arg-Gly-Asp-Phe-Pen-NH2.
abstract: RGD peptides are known as important ligands for integrin receptors in the cell adhesion process. The selectivity of RGD peptides for a certain integrin receptor is partly dependent on the RGD conformation and the residues surrounding the RGD sequence. This paper investigates the effect of the addition of a phenylalanine residue on the RGD conformation in cyclo(1,6)Ac-Cys-Arg-Gly-Asp-Phe-Pen-NH2 (1) as compared to the previously studied cyclo(1,5)Ac-Pen-Arg-Gly-Asp-Cys-NH2 (2). The conformational study of peptide 1 was done in aqueous solution using nuclear magnetic resonance (NMR) spectroscopy and molecular dynamics simulations. This work will increase the understanding of the flanking residue's effect in RGD peptides.
authors.affiliation: Department of Pharmaceutical Chemistry, University of Kansas, Lawrence.
authors.forename: T J
authors.initials: TJ
authors.lastname: Siahaan
authors.forename: D
authors.initials: D
authors.lastname: Bruss
authors.forename: N A
authors.initials: NA
authors.lastname: Powell
authors.forename: S
authors.initials: S
authors.lastname: Chakrabarti
authors.forename: M
authors.initials: M
authors.lastname: Conrad
mesh_terms: D000595:Amino Acid Sequence; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D010456:Peptides, Cyclic / Q000138:chemical synthesis / Q000737:chemistry*; D010649:Phenylalanine / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012996:Solutions; D013329:Structure-Activity Relationship; D013816:Thermodynamics; D014867:Water / Q000737:chemistry*
chemical_list: D009842:Oligopeptides; D010456:Peptides, Cyclic; D012996:Solutions; D014867:Water; D010649:Phenylalanine; C047981:arginyl-glycyl-aspartic acid