Molecular Dynamics of Synthetic Flagelliform Silk Fiber Assembly

Autor:	Elíbio L. Rech, André M. Murad, Paula F. Oliveira, Valquiria A Michalczechen-Lacerda, Luciano P. Silva, Sonia Maria de Freitas, Betulia De Morais Souto, Daniela Bittencourt, Randolph V. Lewis
Rok vydání:	2020
Předmět:	chemistry.chemical_classification Materials science Polymers and Plastics Spidroin General Chemical Engineering Organic Chemistry Article Amino acid Molecular dynamics SILK chemistry Materials Chemistry Biophysics Spider silk Fiber Polyproline helix Flag (geometry)
Zdroj:	Macromol Mater Eng
ISSN:	1439-2054 1438-7492
Popis:	In order to better understand the relationship between Flagelliform (Flag) spider silk molecular structural organization and the mechanisms of fiber assembly, it was designed and produced the Nephilengys cruentata Flag spidroin analogue rNcFlag2222. The recombinant proteins are composed by the elastic repetitive glycine-rich motifs (GPGGX/GGX) and the spacer region, rich in hydrophilic charged amino acids, present at the native silk spidroin. Using different approaches for nanomolecular protein analysis, the structural data of rNcFlag2222 recombinant proteins were compared in its fibrillar and in its fully solvated states. Based on the results was possible to identify the molecular structural dynamics of NcFlag2222 prior to and after fiber formation. Overal rNcFlag2222 shows a mixture of semiflexible and rigid conformations, characterized mostly by the presence of PPII, β-turn and β-sheet. These results agree with previous studies and bring insights about the molecular mechanisms that might driven Flag silk fibers assembly and elastomeric behavior.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::332f1cdf838e591b6e2fdb7b3e375cda https://doi.org/10.1002/mame.202000530 Zobrazit plný text záznamu Plný text