Folded structures of L-leucylglycine oligopeptides and their aggregational behavior in aqueous solution: Raman scattering spectra and proton NMR spin-lattice relaxation studies.
The aggregational behavior of three L-leucylglycine oligopeptides (residue numbers of glycine are 3, 4, and 5) in aqueous solution was investigated by the use of Raman scattering and 1H NMR spin-lattice relaxation methods. The results indicate that their oligopeptides take up a folded structure to form dimeric aggregates above their critical aggregation concentration. The application of one-dimensional aggregate theory to these systems provides the following prediction. Elongation up to 6 glycine residues makes it possible to form dimeric aggregates, but further elongation (up to 7 glycine residues) makes the aggregates very unstable, and up to 8 or 9 glycine residues makes the formation of dimeric aggregates very difficult. The one-dimensional aggregate theory may be used to predict the existence of peptide aggregates through intermolecular hydrogen bonding.
Yoshino
Aki-Hiro
AH
Department of Applied Chemistry, Nagoya Institute of Technology, Gokiso-cho, Showa-ku, Nagoya, Aichi 466-8555, Japan.
Okabayashi
Hiro-Fumi
HF
Kanbe
Hide-Hiro
HH
Suzuki
Keita
K
O'Connor
Charmian J
CJ
D019281:Dimerization; D004151:Dipeptides / Q000737:chemistry* / Q000378:metabolism*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D009842:Oligopeptides / Q000737:chemistry* / Q000378:metabolism*; D017510:Protein Folding; D011522:Protons; D012996:Solutions; D013059:Spectrum Analysis, Raman
D004151:Dipeptides; D009842:Oligopeptides; D011522:Protons; D012996:Solutions; C015905:glycylleucine