Synthesis and solubility properties of peptide fragments of human hemoglobin α‐chain (123‐136)
- 1 September 1988
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 32 (3), 200-207
- https://doi.org/10.1111/j.1399-3011.1988.tb00935.x
Abstract
The solubility prediction method for protected peptides was successfully applied to relatively small peptide fragments of human hemoglobin α-chain (123-136) which contained various polar amino acid residues such as Asp(OBzl), Glu(OBzl), Lys(Z), Ser(Bzl), and Thr(Bzl). As reported previously for hydrophobic peptides and human proinsulin C-peptide fragments, solubility data indicated that the insolubility of protected peptides having a value below 0.90 appeared to begin at the octa- or nonapeptide sequence level and that β-sheet structure played an important role in the insolubility of peptides. When a peptide has a β-sheet structure in the solid state, we can clearly determine the critical chain length for peptide insolubility, the solubility dependence on solvent properties, and the solubility independence of amino acid compositions of peptides.Keywords
This publication has 17 references indexed in Scilit:
- Infrared Absorption Study of Peptide Fragments of Human Hemoglobin α-Chain (123–136) in the Solid StateBulletin of the Chemical Society of Japan, 1987
- α‐Helical oligopeptides with hydrophobic side chains soluble in lipophilic solventsBiopolymers, 1986
- Critical Peptide Size for Insolubility Caused by a β-Sheet Aggregation and Solubility Improvement in Hydrophobic Peptides by Replacement of Alanine Residues with α-Aminoisobutyric Acid ResiduesBulletin of the Chemical Society of Japan, 1985
- The Ability of an α-Aminoisobutyric Acid Residue to Promote Helical Folding in OligopeptidesBulletin of the Chemical Society of Japan, 1985
- Syntheses and Properties of Oligo-l-leucines Containing α-Aminoisobutyric Acid Residues. The Novel Strategy for Solubility Improvement in Helical Oligopeptides Based on the Restriction of the Values of the Backbone Dihedral Angles φ and ψ of α-Aminoisobutyric Acid ResiduesBulletin of the Chemical Society of Japan, 1985
- Conformational analysis of linear peptides. 2. A vapor-pressure osmometry study of self-association in chloroformJournal of the American Chemical Society, 1980
- Association studies ofN-acetyl-amino acidN,N-dimethylamides in carbon tetrachlorideBiopolymers, 1979
- Structure of horse carbonmonoxyhaemoglobinJournal of Molecular Biology, 1976
- Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteinsBiochemistry, 1974
- Intermolecular association by vapor pressure osmometry: A physical chemistry experimentJournal of Chemical Education, 1968