TY - JOUR
T1 - Lipidation Alters the Structure and Hydration of Myristoylated Intrinsically Disordered Proteins
AU - Ji, Jingjing
AU - Hossain, Md Shahadat
AU - Krueger, Emily N.
AU - Zhang, Zhe
AU - Nangia, Shivangi
AU - Carpentier, Britnie
AU - Martel, Mae
AU - Nangia, Shikha
AU - Mozhdehi, Davoud
N1 - Funding Information:
Cryo-TEM imaging was conducted at Cornell Center for Materials Research Shared Facilities, which is supported through the NSF MRSEC program (DMR-1719875). The authors thank Dr. Mariena S. Ramos for obtaining cryo-TEM images. Computational resources were provided by Information and Technology Services at Syracuse University and Extreme Science and Engineering Discovery Environment (XSEDE), which is supported by National Science Foundation grant number ACI-1053575. Anton 2 computer time was provided by the Pittsburgh Supercomputing Center (PSC) through Grant R01GM116961 from the National Institutes of Health. The Anton 2 machine at PSC was generously made available by D.E. Shaw Research. The authors thank Chilkoti group for generous gift of plasmids encoding V and V (Addgene plasmid # 67014). 20 30
Funding Information:
Cryo-TEM imaging was conducted at Cornell Center for Materials Research Shared Facilities, which is supported through the NSF MRSEC program (DMR-1719875). The authors thank Dr. Mariena S. Ramos for obtaining cryo-TEM images. Computational resources were provided by Information and Technology Services at Syracuse University and Extreme Science and Engineering Discovery Environment (XSEDE), which is supported by National Science Foundation grant number ACI-1053575. Anton 2 computer time was provided by the Pittsburgh Supercomputing Center (PSC) through Grant R01GM116961 from the National Institutes of Health. The Anton 2 machine at PSC was generously made available by D.E. Shaw Research. The authors thank Chilkoti group for generous gift of plasmids encoding V20 and V30 (Addgene plasmid # 67014). National Institutes of Health grant R35GM142899 (D.M), NSF-DMR-BMAT-2105193 (D.M. and S.N.), ACS-PRF 61198-DNI (D.M.), NSF-DMR-XC-1757749 and 2049793 (S.N.), NSF-MCB-2221796 (S.N.).
Publisher Copyright:
© 2023 The Authors. Published by American Chemical Society.
PY - 2023/3/13
Y1 - 2023/3/13
N2 - Lipidated proteins are an emerging class of hybrid biomaterials that can integrate the functional capabilities of proteins into precisely engineered nano-biomaterials with potential applications in biotechnology, nanoscience, and biomedical engineering. For instance, fatty-acid-modified elastin-like polypeptides (FAMEs) combine the hierarchical assembly of lipids with the thermoresponsive character of elastin-like polypeptides (ELPs) to form nanocarriers with emergent temperature-dependent structural (shape or size) characteristics. Here, we report the biophysical underpinnings of thermoresponsive behavior of FAMEs using computational nanoscopy, spectroscopy, scattering, and microscopy. This integrated approach revealed that temperature and molecular syntax alter the structure, contact, and hydration of lipid, lipidation site, and protein, aligning with the changes in the nanomorphology of FAMEs. These findings enable a better understanding of the biophysical consequence of lipidation in biology and the rational design of the biomaterials and therapeutics that rival the exquisite hierarchy and capabilities of biological systems.
AB - Lipidated proteins are an emerging class of hybrid biomaterials that can integrate the functional capabilities of proteins into precisely engineered nano-biomaterials with potential applications in biotechnology, nanoscience, and biomedical engineering. For instance, fatty-acid-modified elastin-like polypeptides (FAMEs) combine the hierarchical assembly of lipids with the thermoresponsive character of elastin-like polypeptides (ELPs) to form nanocarriers with emergent temperature-dependent structural (shape or size) characteristics. Here, we report the biophysical underpinnings of thermoresponsive behavior of FAMEs using computational nanoscopy, spectroscopy, scattering, and microscopy. This integrated approach revealed that temperature and molecular syntax alter the structure, contact, and hydration of lipid, lipidation site, and protein, aligning with the changes in the nanomorphology of FAMEs. These findings enable a better understanding of the biophysical consequence of lipidation in biology and the rational design of the biomaterials and therapeutics that rival the exquisite hierarchy and capabilities of biological systems.
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U2 - 10.1021/acs.biomac.2c01309
DO - 10.1021/acs.biomac.2c01309
M3 - Article
C2 - 36757021
AN - SCOPUS:85148037953
SN - 1525-7797
VL - 24
SP - 1244
EP - 1257
JO - Biomacromolecules
JF - Biomacromolecules
IS - 3
ER -