Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 430, Issue 20, Pages 3774-3783Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2018.06.042
Keywords
silkmoth eggshell; silkmoth chorion proteins; tandem repeats; functional amyloids
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Funding
- National and Kapodistrian University of Athens
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Silkmoth chorion is a fibrous structure composed mainly of two major protein classes, families A and B. Both families of silkmoth chorion proteins present a highly conserved, in sequence and in length, central domain, consisting of Gly-rich tandem hexapeptide repetitive segments, flanked by two more variable N-terminal and C-terminal arms. Primary studies identified silkmoth chorion as a functional protective amyloid by unveiling the amyloidogenic properties of the central domain of both protein families. In this work, we attempt to detect the principal source of amyloidogenicity of the central domain by focusing on the role of the tandem hexapeptide sequence repeats. Concurrently, we discuss a possible mechanism for the self-assembly of class A protofilaments, suggesting that the aggregation-prone hexapeptide building blocks may fold into a triangle-shaped beta-helical structure. (C) 2018 Elsevier Ltd. All rights reserved.
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