TY - JOUR
T1 - Composition of Minor Ampullate Silk Makes Its Properties Different from Those of Major Ampullate Silk
AU - Nakamura, Hiroyuki
AU - Kono, Nobuaki
AU - Mori, Masaru
AU - Masunaga, Hiroyasu
AU - Numata, Keiji
AU - Arakawa, Kazuharu
N1 - Funding Information:
This work was supported by a grant from the ImPACT Program of the Council for Science, Technology and Innovation (Cabinet Office, Government of Japan), MEXT Program: Data Creation and Utilization-Type Material Research and Development Project grant number JPMXP1122714694, and by research funds from the Yamagata Prefectural Government and Tsuruoka City, Japan.
Publisher Copyright:
© 2023 American Chemical Society.
PY - 2023/5/8
Y1 - 2023/5/8
N2 - Spider’s minor ampullate silk, or MI-silk, exhibits distinct mechanical properties and water resistance compared to its major ampullate counterpart (MA-silk). The principal protein constituent of MI-silk is known as minor ampullate spidroin, or MiSp, and while its sequence has been deciphered and is thought to underlie the differences in properties with MA-silk, the composition of MI-silk and the relationship between its composition and properties remain elusive. In this study, we set out to investigate the mechanical properties, water resistance, and proteome of MA-silk and MI-silk from Araneus ventricosus and Trichonephila clavata. We also synthesized artificial fibers from major ampullate spidroin, MaSp1 and 2, and MiSp to compare their properties. Our proteomic analysis reveals that the MI-silk of both araneids is composed of MiSp, MaSp1, and spidroin constituting elements (SpiCEs). The absence of MaSp2 in the MI-silk proteome and the comparison of the water resistance of artificial fibers suggest that the presence of MaSp2 is the reason for the disparity in water resistance between MI-silk and MA-silk.
AB - Spider’s minor ampullate silk, or MI-silk, exhibits distinct mechanical properties and water resistance compared to its major ampullate counterpart (MA-silk). The principal protein constituent of MI-silk is known as minor ampullate spidroin, or MiSp, and while its sequence has been deciphered and is thought to underlie the differences in properties with MA-silk, the composition of MI-silk and the relationship between its composition and properties remain elusive. In this study, we set out to investigate the mechanical properties, water resistance, and proteome of MA-silk and MI-silk from Araneus ventricosus and Trichonephila clavata. We also synthesized artificial fibers from major ampullate spidroin, MaSp1 and 2, and MiSp to compare their properties. Our proteomic analysis reveals that the MI-silk of both araneids is composed of MiSp, MaSp1, and spidroin constituting elements (SpiCEs). The absence of MaSp2 in the MI-silk proteome and the comparison of the water resistance of artificial fibers suggest that the presence of MaSp2 is the reason for the disparity in water resistance between MI-silk and MA-silk.
UR - http://www.scopus.com/inward/record.url?scp=85151862794&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85151862794&partnerID=8YFLogxK
U2 - 10.1021/acs.biomac.2c01474
DO - 10.1021/acs.biomac.2c01474
M3 - Article
C2 - 37002945
AN - SCOPUS:85151862794
SN - 1525-7797
VL - 24
SP - 2042
EP - 2051
JO - Biomacromolecules
JF - Biomacromolecules
IS - 5
ER -