Structural Characterization and 5′-mononucleotide Binding of Polyalanine β-sheet Complexes
Article
Pérez-Payá, E, Forood, B, Houghten, RA et al. (1996). Structural Characterization and 5′-mononucleotide Binding of Polyalanine β-sheet Complexes
. JOURNAL OF MOLECULAR RECOGNITION, 9(5-6), 488-493. 10.1002/(SICI)1099-1352(199634/12)9:5/6<488::AID-JMR289>3.0.CO;2-F
Pérez-Payá, E, Forood, B, Houghten, RA et al. (1996). Structural Characterization and 5′-mononucleotide Binding of Polyalanine β-sheet Complexes
. JOURNAL OF MOLECULAR RECOGNITION, 9(5-6), 488-493. 10.1002/(SICI)1099-1352(199634/12)9:5/6<488::AID-JMR289>3.0.CO;2-F
A study was initiated into the formation and stability of highly soluble β-sheet macrostructures. Such β-sheet macrostructures are useful model systems for the study of the biological function of the hydrophobic core of proteins and for the de novo design of novel catalytic mimics. In the current study, a 16-mer-alanine-based peptide (Ac-KA14K-NH2) that is highly water soluble and adopts an extremely stable macromolecular β-sheet structure was synthesized. A tyrosine-containing analog (Ac-KYA13K-NH2) was used to study the tertiary structure of the complex by circular dichroism spectroscopy, while the influence of the charges on the complex formation and binding affinity was evaluated using a zwitterionic analog (Ac-KEA13KE-NH2). Both the secondary and tertiary structures of the β-sheet complex were stable to denaturants, as demonstrated by far- and near-ultraviolet circular dichroism spectroscopy. Binding studies with mononucleotides have shown that the β-sheet complex binds to molecules through both hydrophobic and electrostatic interactions. These intrinsic properties were found to be a prerequisite for the observed enhanced cleavage of phosphodiester bonds.
