Disease relevance of CCRIS 6043

• Its sequence is PAADLARYRHYINLITRQRY-NH2, and the solution structure was calculated from NMR-derived distance and torsion angle restraints, obtained at 15 degrees C in a solvent mixture of water and 30% (v/v) 1,1,1,3,3,3-hexafluoro-2-propanol, by using DIANA and restrained energy minimisation [1].

High impact information on CCRIS 6043

• Amyloid-beta protofibrils differ from amyloid-beta aggregates induced in dilute hexafluoroisopropanol in stability and morphology [2].
• A second class of soluble Abeta aggregates was generated rapidly (<10 min) in buffered 2% hexafluoroisopropanol (HFIP) [2].
• The addition of methanol and of hexafluoro-2-propanol to 1 in aprotic solvents models the PLP-water interaction in the enzymatic active site [3].
• The influence of conformation and aggregation on the hydrogen bond donor ability of fluorinated alcohol solvents [1,1,1,3,3,3-hexafluoro-2-propanol (HFIP) and 1-phenyl-2,2,2-trifluoroethanol (PhTFE)] was explored theoretically (DFT) and experimentally (NMR, kinetics, crystal structure analyses) [4].
• The Raman spectra of alpha-synuclein, a prototypical natively unfolded protein, were obtained in the presence and absence of methanol, sodium dodecyl sulfate (SDS), and hexafluoro-2-propanol (HFIP) [5].

Biological context of CCRIS 6043

• METHODS: After enzymatic hydrolysis of conjugates, hexafluoroisopropanol is detected readily using a head space gas chromatographic analysis with a flame ionization detector [6].
• Electrospinning of type I collagen in 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP) to fabricate a biomimetic nanofibrous extracellular matrix for tissue engineering was investigated [7].
• Hexafluoro-2-propanol (HFIP) was a better helix enhancer in all cases however, the relative effectiveness varied with the peptide sequence [8].
• It turned out that these transmembrane peptides either in hexafluoroisopropanol or cast from it take an ordinary alpha-helix (alpha(I)-helix) irrespective of their amino acid sequences with reference to the conformation-dependent (13)C chemical shifts of (Ala)(n) taking the alpha-helix form [9].

Anatomical context of CCRIS 6043

• Micellar aggregates formed following the addition of hexafluoroisopropanol to phospholipid membranes [10].

Associations of CCRIS 6043 with other chemical compounds

• Although K3 formed an alpha-helix at high concentrations of 2,2,2-trifluoroethanol (TFE) and 1,1,1,3,3,3-hexafluoroisopropanol (HFIP) in 10 mM HCl (pH approximately 2), the helical content was not high, indicating a low preference to do so [11].
• Fluoride and HFIP were quantitated using an ion-selective electrode and by gas chromatography, respectively [12].
• The syntheses involved the reaction of PMB-protected d- and l- seleno-, thio-, and iminoarabinitol with a benzylidene- and isopropylidene-protected 1,3-cyclic sulfate, derived from commercially available d-sorbitol, in 1,1,1,3,3,3-hexafluoro-2-propanol containing potassium carbonate [13].
• FA, TFA, and HFIP treatments modify the secondary structure of collagen, as shown by Fourier transform infrared spectroscopy, while TFE does not [14].
• Intrinsic tryptophan fluorescence studies, ANS binding and near UV-CD experiments indicate the protein is more expanded, have more exposed hydrophobic surfaces and highly disrupted tertiary structure at 60% (v/v) TFE and 30% (v/v) HFIP concentrations [15].

Gene context of CCRIS 6043

• As the concentration of HFIP was increased, the beta-sheet content and proteinase K resistance of PrP27-30 as well as prion infectivity diminished [16].
• Aggregated IAPP can be resolubilized by HFIP or DMSO and recovered by HPLC with very good yield [17].
• The three-dimensional structure of a synthetic fragment of human apolipoprotein CII (apo-CII) in 35%, 1,1,1,3,3,3-hexafluoro-2-propanol (HFP) has been determined on the basis of distance and intensity constraints derived from two-dimensional proton nuclear magnetic resonance measurements [18].
• As the concentration of HFIP was increased, the beta-sheet content and proteinase K resistance of PrP 27-30 as well as prion infectivity diminished [19].
• A model of the structure of the 22 amino acid residue gastrointestinal peptide hormone motilin in 30% hexafluoro-2-propanol has been obtained by using distance constraints obtained from two-dimensional nuclear Overhauser enhancements [20].

Analytical, diagnostic and therapeutic context of CCRIS 6043

• Circular dichroism spectra indicate the presence of alpha-helical secondary structure in aqueous solution, and the secondary structure can be stabilized with hexafluoro-2-propanol [21].
• Moreover, the characterizations of rANF(99-126) and the analog pBNP1, which combines the cyclic core of bBNP32 with the carboxy- and amino-terminal segments of rANF-(99-126), have been carried out by Fourier transform infrared spectroscopy (FTIR) in 40% HFIP/D2O [22].
• Size-exclusion chromatography in 1,1,1,3,3,3-hexafluoro-2-propanol [23].
• After lyophilization, QUIN and [18O]QUIN were esterified with hexafluoroisopropanol (to mass 467 and 471, respectively) using trifluoroacetylimidazole as catalyst [24].
• After centrifugation, aliquots of the supernatants were dried and the resulting residues were derivatized in a single step with heptafluorobutyric anhydride and hexafluoroisopropanol [25].

References