Self‐assembling peptides are a popular vector for therapeutic cargo delivery due to their versatility, tunability, and biocompatibility. Accurately predicting secondary and supramolecular structures of self‐assembling peptides is essential for de novo peptide design. However, computational modeling of such assemblies is not yet able to accurately predict structure formation for many peptide sequences. This review identifies patterns in literature between secondary and supramolecular structures, primary sequences, and applications to provide a guide for informed peptide design. An overview of peptide structures, their applications as nanocarriers, and analytical methods for characterizing secondary and supramolecular structure is examined. A top‐down approach is then used to identify trends between peptide sequence and assembly structure from the current literature, including an analysis of the drivers at work, such as local and nonlocal sequence effects and solution conditions.
This content will become publicly available on December 28, 2024
The assembly of peptide and peptide‐inspired building blocks into functional, well‐defined, multi‐length scale materials represents an exciting, rapidly expanding research field that bridges the principles of polymer science and engineering with a tremendous breadth of biomolecular interactions. The advantageous features of peptides, including their biocompatibility, functional diversity, and high purity, are complemented by the breadth of potential applications that may arise from their resultant structures and assemblies. Applications in biology (tissue scaffolding and drug conjugation), electronics (electron and/or ion‐conduction), and membranes (ion capture and ultrafiltration) represent a few of many examples where such biologically rich materials hold potential for enabling new routes to enhanced materials performance. Achieving successful solution and interfacial assembly techniques for peptides and other peptidomimetic materials requires obtaining a deep understanding of their design principles and limitations, as well as their amenability to structure formation when subjected to a variety of environmental conditions, such as pH, solvent, and temperature, to which such assembly methods may be exquisitely sensitive. This review especially focuses on mechanisms and the product of oligo‐ and polypeptide assembly, often resulting in the formation of extended, wire‐like structures obtained by solution methods, with inclusion of peptoid‐based structures and the complementary roles of polymerizations and step‐by‐step synthetic methods. Moreover, we describe relationships between naturally occurring peptide‐based structures, such as
- NSF-PAR ID:
- 10482771
- Publisher / Repository:
- Wiley Blackwell (John Wiley & Sons)
- Date Published:
- Journal Name:
- Journal of Polymer Science
- ISSN:
- 2642-4150
- Format(s):
- Medium: X
- Sponsoring Org:
- National Science Foundation
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