Switch-peptides as folding precursors in self-assembling peptides and amyloid fibrillogenesis
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Conformational transitions of peptides and proteins have recently moved to the center of interest in various domains of research at the interface of chemistry, biology, and medicine due to their implication in an increasing number of diseases in which the ...
Aspects of conformational transitions, folding, and misfolding of peptides and proteins have recently taken center stage in various domains at the interface of chemistry, biology, and medicine because of their impact on protein misfolding diseases. Due to ...
Numerous human diseases are associated with conformational change and aggregation of proteins, including Alzheimer's, Parkinson's, prion diseases (such as mad cow disease), familial amyotrophic lateral sclerosis (ALS, or Lou Gehrig's disease), Huntington's ...
Deciphering the mechanism(s) of beta-sheet mediated self-assembly is essential for understanding amyloid fibril formation and for the fabrication of polypeptide materials. Herein, we report a simple peptidomimetic that self-assembles into polymorphic beta- ...
Temp.-dependent NMR and CD spectra of MeOH solns. of a beta-hexapeptide and of a beta-heptapeptide between 298 and 393 K are reported. They establish the fact that the 314-helical secondary structures of the 2 beta-peptides do not "melt" in the temp. range ...
Amyloid plaques in brain, composed of aggregates of amyloid-beta peptide, play a central role in the pathogenesis of Alzheimer's disease and represent a good target for treatment. We have shown previously that a 5-amino acid beta-sheet breaker peptide (iAb ...
A novel concept for triggering conformational transitions, and thus changes in structure and function, in peptides with a switching element S provides intriguing perspectives for studying mol. processes that play a key role, for example, in early events of ...
Alzheimer's disease (AD) is a progressive neurodegenerative disorder with clinical manifestations appearing in old age, however, the initial stages of this disease may begin early in life. AD is characterized by the presence of excessive deposits of aggreg ...
Federation of American Society of Experimental Biology2005
Studies have indicated that partially unfolded states occur under conditions that favor amyloid formation by transthyretin (TTR), as well as other amyloidogenic proteins. In this study, we used hydrogen exchange measurements to show that there is selective ...
Intramol. O,N-acyl migration reactions were used as structural switch (S-elements) from a depsipeptide bond contg., unfolded state (Soff) to an all-amide, native states (Son). Chem. or enzymically triggered acyl migrations allowed for the controlled induct ...
