Syntheses and properties of oligo-L-leucines containing .ALPHA.-aminoisobutyric acid residues. The novel strategy for solubility improvement in helical oligopeptides based on the restriction of the values of the backbone dihedral angles .PHI. and .PSI. of
スポンサーリンク
概要
- 論文の詳細を見る
In order to provide a succinct demonstration of the usefulness of a new strategy for solubility improvement in protected peptide fragments included in α-helical regions of proteins, model oligo(Leu)s containing Aib or Ala residues were prepared by stepwise elongation and fragment condensation methods. The peptides prepared were the following: Boc–(Leu<SUB>3</SUB>–Aib)<I><SUB>n</SUB></I>–OBzl, Boc–(Leu<SUB>4</SUB>–Aib)<I><SUB>n</SUB></I>–OBzl, and Boc–(leu<SUB>3</SUB>–Ala)<I><SUB>n</SUB></I>OBzl (<I>n</I>=1–3). Carboxyl component peptides having Aib residues at the C-terminals smoothly reacted with amino component peptides in high yields with no care of racemization due to the absence of chiral centers in Aib residues. As expected, peptides containing Aib residues have high solubility in moderate- and high-polar organic solvents and are easily purified by recrystallization from aqueous ethanol. This is in remarkable contrast with the result that the octa- and dodecapeptides containing Ala residues are barely soluble or insoluble in these solvents. Conformational analyses by IR spectroscopies indicated that Boc–(Leu<SUB>3</SUB>–Aib)<I><SUB>n</SUB></I>–OBzl and Boc–(Leu<SUB>4</SUB>–Aib)<I><SUB>n</SUB></I>–OBzl (<I>n</I>=2 and 3) had helical conformations (3<SUB>10</SUB>- or α-helices) in dichloromethane, whereas Boc–(Leu<SUB>3</SUB>–Ala)<I><SUB>n</SUB></I>–OBzl (<I>n</I>=2 and 3) had fully developed β-sheet structures in the solid state. The high solubility of the peptides containing Aib residues is explained by the observation that replacement of C<SUP>α</SUP> hydrogen atoms with methyl groups greatly disturbs β-sheet structures, promoting helical folding in peptides. The implications of the new findings for the chemistry of peptides and proteins containing α,α-disubstituted α-amino acid residues is also discussed by building up a CPK model of an α-helical structure.
- 公益社団法人 日本化学会の論文
著者
-
Narita Mitsuaki
Department Of Biotechnology And Life Science Faculty Of Technology Tokyo University Of Agriculture A
-
Ishikawa Kazunori
Department Of Cardiovascular Surgery Division Of Heart Institute Sendai Kosei Hospital
-
Doi Masamitsu
Department of Industrial Chemistry, Faculty of Technology, Tokyo University of Agriculture and Technology
-
Sugasawa Hiroki
Department of Industrial Chemistry, Faculty of Technology, Tokyo University of Agriculture and Technology
関連論文
- Left ventricular lipoma with pseudoaneurysm-like appearance
- 電導度検出に基づく有機リン系殺虫剤の新しい酵素分析法の開発
- Single Amino Acid Preferences for Specific Locations at Type-I α-Turns in Globular Proteins
- A New Type of Φ, Ψ Representation of the Protein Tertiary Structure and the Analysis of the Amino Acid Preferences for Speciffic Locations at Type-II β-Turn by Using 8000 Possible Kinds of Amino Acid Residues
- Statistical Characterization of Eleven Kinds of Helix Elements with Amino Acid Residues in the Middle of Triplets
- Conformations of Synthetic Model Peptides for Plasmodium falciparum Circumsporozoite Protein in Me_2SO by ^1H NMR and Distance Geometry Calculations
- Effect of Hydration on the Thermal Stability of the Collagen Model Peptide Containing 4(S)-Hydroxyproline
- Only Weak Dependence of the Protected Peptides Solubility in Organic Solvents on Their Amino Acid Sequence
- The Influence of Protecting Groups on the β-Sheet-Structure Stability of Protected Peptides^
- Surgical Treatment for Primary Cardiac Leiomyosarcoma Causing Right Ventricular Outflow Obstruction
- Assingments of Tri- and Tetrapeptide Sequences in Globular Proteins to the 18 Kinds of Local Structures along Helices and Their Propensities for Specific Local Structures
- Fully supported open stent grafting applied with a Matsui-Kitamura (MK) stent in treatment of distal arch aneurysm
- The Crystal Structure of the Collagen Model Peptide containing 4(S)-hydroxyproline-proline-glycine Repeats
- Acute Aortic Regurgitation due to Local Avulsion of the Aortic Valve Commissure
- Syntheses and properties of oligo-L-leucines containing .ALPHA.-aminoisobutyric acid residues. The novel strategy for solubility improvement in helical oligopeptides based on the restriction of the values of the backbone dihedral angles .PHI. and .PSI. of
- The ability of an .ALPHA.-aminoisobutyric acid residue to promote helical folding in oligopeptides.
- Individuality of amino acid residues in protected peptides. Conformational and .BETA.-sheet structure-disrupted behaviors of resin-bound peptides.
- Conformations in the solid state and solubility properties of protected homooligopeptides of glycine and .BETA.-alanine.
- Liquid phase peptide synthesis by fragment condensation on soluble polymer support. IV. Relative reactivities of N-t-butoxycarbonyl(Boc)amino acids and Boc-oligopeptide acids in their esterification with soluble chloromethylated polystyrene.
- Liquid-phase peptide synthesis by fragment condensation on a soluble polymer support. III. The influence of the content and the chain length of a peptide anchored to a soluble polymer support on the reactivity of the amino-free terminal of the peptide.
- Infrared absorption study of human hemoglobin .ALPHA.-chain (123-136) fragments in dichloromethane.
- Critical peptide size for insolubility caused by a .BETA.-sheet aggregation and solubility improvement in hydrophobic peptides by replacement of alanine residues with .ALPHA.-aminoisobutyric acid residues.
- Design of the synthetic route for helical peptides. Synthesis and solubility of model peptides having a helical structure.
- The easy disruption of the .BETA.-sheet structure of resin-bound human proinsulin C-peptide fragments by strong electron-donor solvents.
- Infrared absorption study of human proinsulin C-peptide fragments in dichloromethane.
- The electron donor-acceptor interaction between mixed solvents and its influence on their .BETA.-sheet strucutre-disrupting potential.
- The .BETA.-sheet structure-disrupting potential of electron-donor and -acceptor solvents and role of mixed solvents in solvation of peptides.
- The solubility of peptide intermediates in organic solvents. Solubilizing potential of hexafluoro-2-propanol.
- Infrared absorption study of peptide fragments of human hemoglobin .ALPHA.-chain (123-136) in the solid state.
- Infrared absorption study of human proinsulin C-peptide fragments in the solid state.
- The study on peptide and protein syntheses. Infrared spectroscopic conformational analysis of oligo-L-leucines containing only one D-amino acid residue.
- Liquid phase peptide synthesis by the fragment condensation on soluble polymer support. II. The azide method.
- Liquid phase peptide synthesis by the fragment condensation on soluble polymer support. I. Efficient coupling and relative reactivity of a peptide fragment with various coupling reagents.