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  • 1
    Electronic Resource
    Electronic Resource
    The synthesis and spectroscopic analysis of the neurotoxic prion peptide 106-126: Comparative use of manual Boc and Fmoc chemistry (1999)
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 129-134 
    Details
    ISSN: 1573-3904
    Keywords: amyloid ; circular dichroism ; 'difficult sequence' ; in situ neutralisation ; N-(2-hydroxy-4-methoxybenzyl) ; tetramethylfluoroformamidinium hexafluorophosphate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A peptide corresponding to residues 106-126 of the human prion protein (PrP) possesses the neurotoxic and amyloidogenic properties of the infectious form of the parental protein. This peptide is now identified as a 'difficult sequence' and synthesis using conventional manual Fmoc chemistry was unsuccessful with acylation terminating at a central core of hydrophobic amino acids. The use of tetramethylfluoroformamidinium hexafluorophosphate and 1-methyl-2- pyrrolidone as anti-aggregatory agents in the coupling steps improved the synthesis but still resulted in an incomplete peptide. The incorporation of N-(2-hydroxy-4-methoxybenzyl) protection at glycine residues 119 and 124 enabled synthesis of the full length peptide in low yield. Synthesis using Boc chemistry with in situ neutralisation gave the full length peptide in high yield.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008808607811
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Secondary structural modifications of Aβ(1–40) induced by multiple 2-acetoxy-4-methoxybenzyl (acetylHmb) protection (1999)
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 289-293 
    Details
    ISSN: 1573-3904
    Keywords: Aβ(1–40) ; acetylHmb ; circular dichroism ; electron microscopy ; fibril formation ; secondary structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Modifications to secondary structure and fibril formation caused by multiple acetylHmb backbone amide protection of Alzheimer's disease Aβ(1–40) were investigated using circular dichroism spectroscopy and electron microscopy. Penta(acetylHmb) Aβ(1–40) was observed to have a reduced ability to form α-helix and β-sheet structures under the same solution conditions as the native peptide, with α-helical propensity being reduced more significantly than β-sheet propensity. Further, acetylHmb backbone protection was found to alter Aβ(1–40) interaction with SDS-micelles by preventing α-helix formation. Aβ fibril formation, a characteristic property of this peptide, was also not observed for penta(acetylHmb) Aβ(1–40).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02443424
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    The synthesis and spectroscopic analysis of the neurotoxic prion peptide 106–126: Comparative use of manual Boc and Fmoc chemistry (1999)
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 129-134 
    Details
    ISSN: 1573-3904
    Keywords: amyloid ; circular dichroism ; ‘difficult sequence’ ; in situ neutralisation ; N-(2-hydroxy-4-methoxybenzyl) ; tetramethylfluoroformamidinium hexafluorophosphate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary A peptide corresponding to residues 106–126 of the human prion protein (PrP) possesses the neurotoxic and amyloidogenic properties of the infectious form of the parental protein. This peptide is now identified as a ‘difficult sequence’ and synthesis using conventional manual Fmoc chemistry was unsuccessful with acylation terminating at a central core of hydrophobic amino acids. The use of tetramethylfluoroformamidinium hexafluorophosphate and 1-methyl-2-pyrrolidone as anti-aggregatory agents in the coupling steps improved the synthesis but still resulted in an incomplete peptide. The incorporation ofN-(2-hydroxy-4-methoxybenzyl)protection at glycine residues 119 and 124 enabled synthesis of the full length peptide in low yield. Synthesis using Boc chemistry within situ neutralisation gave the full length peptide in high yield.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02443627
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Secondary structural modifications of Aβ(1-40) induced by multiple 2-acetoxy-4-methoxybenzyl (acetylHmb) protection (1999)
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 289-293 
    Details
    ISSN: 1573-3904
    Keywords: Aβ(1-40) ; acetylHmb ; circular dichroism ; electron microscopy ; fibril formation ; secondary structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Modifications to secondary structure and fibril formation caused by multiple acetylHmb backbone amide protection of Alzheimer's disease Aβ(1-40) were investigated using circular dichroism spectroscopy and electron microscopy. Penta(acetylHmb)Aβ(1-40) was observed to have a reduced ability to form α-helix and β-sheet structures under the same solution conditions as the native peptide, with α-helical propensity being reduced more significantly than β-sheet propensity. Further, acetylHmb backbone protection was found to alter Aβ(1-40) interaction with SDS-micelles by preventing α-helix formation. Aβ fibril formation, a characteristic property of this peptide, was also not observed for penta(acetylHmb)Aβ(1-40).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008931309727
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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