TY - JOUR
T1 - Temperature-Responsive Nano-Biomaterials from Genetically Encoded Farnesylated Disordered Proteins
AU - Hossain, Md Shahadat
AU - Zhang, Zhe
AU - Ashok, Sudhat
AU - Jenks, Ashley R.
AU - Lynch, Christopher J.
AU - Hougland, James L.
AU - Mozhdehi, Davoud
N1 - Funding Information:
The development of farnesylation platforms was supported by NIH grants R01GM132606 (J.L.H.) and R35GM142899 (D.M). The soft-matter characterization was partially supported by NSF-DMR-BMAT-2105193 (D.M.). Z.Z. was partially supported by ACS-PRF 61198-DNI (D.M.).
Funding Information:
This work was possible with the generous support of NIH, NSF, and ACS-PRF. The cryo-TEM imaging was conducted at the Cornell Center for Materials Research Shared Facilities, which are supported through the NSF MRSEC program (DMR-1719875). We thank Dr. Mariena S. Ramos for obtaining the TEM images.
Publisher Copyright:
©
PY - 2021
Y1 - 2021
N2 - Despite broad interest in understanding the biological implications of protein farnesylation in regulating different facets of cell biology, the use of this post-translational modification to develop protein-based materials and therapies remains underexplored. The progress has been slow due to the lack of accessible methodologies to generate farnesylated proteins with broad physicochemical diversities rapidly. This limitation, in turn, has hindered the empirical elucidation of farnesylated proteins' sequence-structure-function rules. To address this gap, we genetically engineered prokaryotes to develop operationally simple, high-yield biosynthetic routes to produce farnesylated proteins and revealed determinants of their emergent material properties (nano-aggregation and phase-behavior) using scattering, calorimetry, and microscopy. These outcomes foster the development of farnesylated proteins as recombinant therapeutics or biomaterials with molecularly programmable assembly.
AB - Despite broad interest in understanding the biological implications of protein farnesylation in regulating different facets of cell biology, the use of this post-translational modification to develop protein-based materials and therapies remains underexplored. The progress has been slow due to the lack of accessible methodologies to generate farnesylated proteins with broad physicochemical diversities rapidly. This limitation, in turn, has hindered the empirical elucidation of farnesylated proteins' sequence-structure-function rules. To address this gap, we genetically engineered prokaryotes to develop operationally simple, high-yield biosynthetic routes to produce farnesylated proteins and revealed determinants of their emergent material properties (nano-aggregation and phase-behavior) using scattering, calorimetry, and microscopy. These outcomes foster the development of farnesylated proteins as recombinant therapeutics or biomaterials with molecularly programmable assembly.
KW - bioconjugation
KW - farnesylation
KW - lipidated biopolymers
KW - lipidation
KW - post-translational modification
KW - recombinant nano-biomaterials
KW - self-assembly
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U2 - 10.1021/acsabm.1c01162
DO - 10.1021/acsabm.1c01162
M3 - Article
C2 - 35044146
AN - SCOPUS:85123823217
SN - 2576-6422
JO - ACS Applied Bio Materials
JF - ACS Applied Bio Materials
ER -