title: Structure of A beta(25-35) peptide in different environments.
abstract: The fragment A beta(25-35) of the Alzheimer's amyloid beta-peptide, like its full-length peptide A beta(1-42), has shown neurotoxic activities in cultured cells. The conformational preference of this important peptide is examined here in solution, gel, and film states (obtained with organic and aqueous solvents) by vibrational circular dichroism spectroscopy for the first time. For comparative studies, vibrational absorption and electronic circular dichroism measurements were also carried out under identical conditions. The peptide was found to adopt beta-sheet and beta-turn structures, with their relative proportions changing in different environments.
authors.affiliation: Department of Chemistry, Vanderbilt University, Nashville, Tennessee 37235, USA.
authors.forename: Ganesh
authors.initials: G
authors.lastname: Shanmugam
authors.forename: Prasad L
authors.initials: PL
authors.lastname: Polavarapu
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry*; D002942:Circular Dichroism; D004777:Environment; D005782:Gels / Q000737:chemistry; D044367:Phase Transition; D011487:Protein Conformation; D012997:Solvents / Q000737:chemistry*
chemical_list: D016229:Amyloid beta-Peptides; D005782:Gels; D012997:Solvents; C439320:amyloid beta-protein (25-36)