Fine structural tuning of the assembly of ECM peptide conjugates via slight sequence modifications.
Fine structural tuning of the assembly of ECM peptide conjugates via slight sequence modifications.
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DOI:
10.1126/sciadv.abd3033
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发表时间:
2020-10
期刊:
影响因子:
13.6
通讯作者:
Kiick KL
中科院分区:
文献类型:
--
作者:
Qin J;Sloppy JD;Kiick KL
The thermoresponsiveness and structures of peptide-based nanocarriers can be altered to enable versatile mechanisms of cargo delivery. The self-assembly of nanostructures from conjugates of elastin-like peptides and collagen-like peptides (ELP-CLP) has been studied as means to produce thermoresponsive, collagen-binding drug delivery vehicles. Motivated by our previous work in which ELP-CLP conjugates successfully self-assembled into vesicles and platelet-like nanostructures, here, we extend our library of ELP-CLP bioconjugates to a series of tryptophan/phenylalanine-containing ELPs and GPO-based CLPs [W2Fx-b-(GPO)y] with various domain lengths to determine the impact of these modifications on the thermoresponsiveness and morphology. The lower transition temperature of the conjugates with longer ELP or CLP domains enables the formation of well-defined nanoparticles near physiological temperature. Moreover, the morphological transition from vesicles to platelet-like nanostructures occurred when the ratio of the lengths of ELP/CLP decreased. Given the previously demonstrated ability of many ELP-CLP bioconjugates to bind to both hydrophobic drugs and collagen-containing materials, our results suggest new opportunities for designing specific thermoresponsive nanostructures for targeted biological applications.
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