Abstract
Intrinsically disordered proteins have dramatically changed the structure–function paradigm of proteins in the 21st century. Resilin is a native elastic insect protein, which features intrinsically disordered structure, unusual multi-stimuli responsiveness and outstanding resilience. Advances in computational techniques, polypeptide synthesis methods and modular protein engineering routines have led to the development of novel resilin-like polypeptides (RLPs) including modular RLPs, expanding their applications in tissue engineering, drug delivery, bioimaging, biosensors, catalysis and bioelectronics. However, how the responsive behaviour of RLPs is encoded in the amino acid sequence level remains elusive. This review summarises the milestones of RLPs, and discusses the development of modular RLP-based biomaterials, their current applications, challenges and future perspectives. A perspective of future research is that sequence and responsiveness profiling of RLPs can provide a new platform for the design and development of new modular RLP-based biomaterials with programmable structure, properties and functions.
Highlights
Disordered proteins have dramatically changed the structure–function paradigm of proteins in the 21st century
The amino acid sequence of resilin was first identified in early 2000s from the CG15920 gene segment of the fruit fly Drosophila melanogaster, which opened up new opportunities for synthesis and development of biomimetic resilins[11]
The first recombinant pro-resilin or resilin-like polypeptide (RLP), namely Rec1-resilin was synthesized in mid-2000s as a water soluble polypeptide expressed in the bacteria Escherichia coli[12]
Summary
● Unique sequence rich in uncharged, polar amino acids and devoid of canonical hydrophobic residues, and contains higher proportion of glycine- and proline-rich segments. On the other hand, when a trimeric modular RLP, namely REC, or RLP4-ELP7-CLP2 was synthesized and investigated for responsive properties, the modular RLP exhibited predominantly PPII conformation and self-assembled into network of flexible aligned fibres (different from that of the twisted rope-helical structures observed for some glycine-rich ELPs) in water[41], which is similar to that of RES50, and needs further investigation[24]. When the modular RLP—namely RLP4-SLP4—comprising RLP (as soft block) encoded from exon-1 of D. melanogaster gene and SLP (as hard block) was synthesized and investigated for stimuli-responsive properties, the modular RLPs formed spherical micelles (10–20 nm diameter with SLP core) at 4 °C, which readily transformed to nanofibrillar structure (80–200 nm length) at 37 °C and large coalescent nanostructures at 70 °C (observed using AFM)[45]. Increase in lysine crosslinking site and mechanical property aThe RLPs, namely AnX and RZ10 are constructed using the mosquito BX619161 gene, whereas the rest using the fruit fly CG15920 gene
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
