Biological applications of water-soluble polypeptides with ordered secondary structures

Abstract

Herein, recent advances in the synthesis of the water-soluble polypeptides with ordered secondary structures via ring-opening polymerization of NCA/NTA and their biological applications are described.

Studies of cell-penetrating peptides by biophysical methods

“…All these studies fuel the opinion that the helical or at least ordered structure of cationic CPPs enhanced their ability to penetrate cells. The biological application of polypeptides with ordered secondary structures is discussed in more detail in the review (Ge et al ., 2020). These and similar observations raised the idea to stabilize the helix structure in CPPs to improve cargo delivery into cells.…”

A call for action to the biomaterial community to tackle antimicrobial resistance

“…76 A specific notable example of the flexibility of more modern HDPs can be seen in the nylon-3 polymers development by Liu et al 77 These multifunctional polymers are capable of fine tuning the hydrophobicity, charge density, and conformational propensity of the material to selectively target specific bacteria while pro-viding low hemolysis and minimal cytotoxicity. Further broad advancements in HDPs may be found in reviews by Ding et al, 68 Haney et al 74 and Ge et al 78 Albeit promising, historically these types of antimicrobials have had significant disadvantages, such as short or limited periods of activity, tissue toxicity, high manufacturing costs and a poor ability to function in an ever changing healthcare environment. 73 However, given the current global AMR problem, these technologies are re-emerging within the biomaterials community with hope that they offer a new generation of antimicrobials and antimicrobial devices.…”

Highly Tough, Stretchable, and Enzymatically Degradable Hydrogels Modulated by Bioinspired Hydrophobic β-Sheet Peptides

“…Among these, the construction of highly ordered β-sheet or α-helix secondary structures endows natural materials with excellent mechanical properties. 2,3 For example, spider-silk has a super tensile strength of 300−800 MPa through the precise arrangement of the hydrophobic sequence GAGAGSGAAG[SG(AG) 2 ] 8 Y, which forms a highly ordered β-sheet assembly through parallel hydrogen bonding. 4,5 Inspired by natural materials, various peptides with highly ordered secondary structures have been used to enhance hydrogel networks.…”

“…Nature is the best teacher of human beings; it already has given many solutions to improve the mechanical properties of materials. Among these, the construction of highly ordered β-sheet or α-helix secondary structures endows natural materials with excellent mechanical properties. , For example, spider-silk has a super tensile strength of 300–800 MPa through the precise arrangement of the hydrophobic sequence GAGAGSGAAG­[SG­(AG) 2 ] 8 Y, which forms a highly ordered β-sheet assembly through parallel hydrogen bonding. , …”

“…Inspired by natural materials, various peptides with highly ordered secondary structures have been used to enhance hydrogel networks. − Besides polypeptides that were produced by complex gene encoding, clone, and extraction from bacteria ,, or by N -carboxyanhydride ring-opening polymerization (NCA ROP), ,, it was found that short peptides with only 3–8 amino acids also can self-assemble into highly ordered β-sheet or α-helix , secondary structures by a rational design. Therefore, short peptides that can be highly orderly assembled have attracted great attention due to the easier synthesis, facile functionalization, and stability compared to their longer variants. − Inspired by the microscopic architecture of natural cartilage, Sun et al reported using a β-sheet short peptide supramolecular network to serve as a sacrificial bond to efficiently dissipate energy, so as to improve the mechanical strength of hydrogels .…”