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Its central seven\u2010residue segment KLVFFAE (A\u03b216\u201322), which is thought to be crucial for fibril formation of the full\u2010length peptide, forms fibrils even in isolation. Context\u2010dependent induction of amyloid formation by such sequences in peptides, which otherwise do not have that propensity, is of considerable interest. We have examined the effect of introducing the A\u03b216\u201322 sequence at the N\u2010terminus of two amphipathic helical 18\u2010residue peptides Ac\u2010WYSEMKRNVQRLERAIEE\u2010am and Ac\u2010KQLIRFLKRLDRNLWGLA\u2010am, which have high average hydrophobic moment &lt;\u03bcH&gt; values but have net charges of 0 and +4, respectively, at neutral pH. Upon incubation in aqueous buffer, fibril\u2010like aggregates were discernible by transmission electron microscopy for the peptide with only 0 net charge, which also displayed ThT binding and \u03b2\u2010structure. Although both the sequences have been derived from amphipathic helical segments in globular proteins and possess high average hydrophobic moments, the +4 charge peptide lacks the ability to form fibrils, while the peptide with 0 charge has the tendency to form fibrillar structures. Variation in the net charge and the presence of several glutamic acids in the sequence of the peptide with net charge 0 appear to favor the formation of fibrils when the A\u03b216\u201322 sequence is attached at the N\u2010terminus. 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