In the last decade, after realization that even short amino acid stretches can undergo amyloidogenesis, numerous short peptides of varying length were studied for their amyloid forming propensity. Since the studied systems were simple (comprising of 3-10 amino acids), the residue specific details were easy to obtain (both experimentally and computationally).
Why is it that most of these peptides are hexameric? Is there any particular rationale behind choosing hexapeptides?
Originally , the first of these sequences were obtained by analyzing fragments of natural amyloid forming proteins to identify the sequence determinants of amyloid formation, identifying the shortest fragments that still yield reproducible random-coil - amyloid beta strand transitions, then these sequences were mutated to identify the contributions of individual residues. De novo design of amyloid peptides tested the lessons learned from natural sequences. Those sequences that were demonstrated to work were further analyzed in later studies
https://scholar.google.ch/scholar?hl=en&q=amyloid+formation+model+systems+peptide+length&btnG=&as_sdt=1%2C5&as_sdtp=
Hi Dushyantj just a thought is that the hexahis is easy to to get rid of they affect amuloid sructures
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