title: Conformational behavior of fragments of adrenocorticotropin and their antisense peptides determined by NMR spectroscopy and CD spectropolarimetry.
abstract: An 'antisense' peptide ('HTCA'), whose sequence was generated by reading the antisense RNA sequence corresponding to ACTH (1-24) was shown to bind ACTH (1-24) with a Kd of 0.3 nM in a solid-matrix binding assay [( 1986) Biochem. J. 234, 679 683]. Two-dimensional NMR spectra were used to examine the conformational behavior in methanol and in water solution of two fragments of adrenocorticotropin, ACTH(1-24) and ACTH (1-13), as well as their antisense peptides, HTCA and HTCA(12-24). The conformations are extended chains in these solutions, both as isolated molecules and when mixed with their antisense complements. The Kd values are greater than 1 mM.
authors.affiliation: Howard Hughes Medical Institute, NHLBI, Bethesda, MD 20892.
authors.forename: E S
authors.initials: ES
authors.lastname: Najem
authors.forename: A
authors.initials: A
authors.lastname: Corigliano-Murphy
authors.forename: J A
authors.initials: JA
authors.lastname: Ferretti
mesh_terms: D000324:Adrenocorticotropic Hormone; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides; D011487:Protein Conformation
chemical_list: D010455:Peptides; D000324:Adrenocorticotropic Hormone