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Supramolecular-Covalent Peptides Self-Assembly: From Design to Regenerative Medicine and Beyond.
- Source :
- Biophysica; Dec2022, Vol. 2 Issue 4, p324-339, 16p
- Publication Year :
- 2022
-
Abstract
- The field of supramolecular peptides self-assembly has undergone outstanding growth since the early 1990s after the serendipitously discovery by Shuguang Zhang of an ionic self-complementary peptide as a repeating segment in a yeast protein. From then on, the field expanded at an accelerating pace and these self-assembled materials have become an integral part of a broad plethora of designer supramolecular nanomaterials useful for different applications ranging from 3D tissue cell cultures, regenerative medicine, up to optoelectronics. However, the supramolecular peptide based-nanomaterials available thus far for regenerative medicine still lack the dynamic complexity found in the biological structures that mediate regeneration. Indeed, self-assembling peptide (SAPs) suffer from poor mechanical stability, losing mechanical properties at low strains. Just like the extracellular matrix (ECM) of living systems, the chemical structure of the SAP-biomaterials should concurrently contain non-covalent and covalent bonds, bringing, respectively, infinite and finite lifetimes of interactions to obtain a reversibly dynamic matrix. In this review, will be highlighted the major advantages and current limitations of SAP-based biomaterials, and it will be discussed the most widely used strategies for precisely tune their mechanical properties (stiffness, resilience, strain-failure, stress resistance), describing recent and promising approaches in tissue engineering, regenerative medicine, and beyond. [ABSTRACT FROM AUTHOR]
- Subjects :
- PEPTIDES
REGENERATIVE medicine
OPTOELECTRONICS
ELASTIC modulus
STIFFNESS (Mechanics)
Subjects
Details
- Language :
- English
- ISSN :
- 26734125
- Volume :
- 2
- Issue :
- 4
- Database :
- Complementary Index
- Journal :
- Biophysica
- Publication Type :
- Academic Journal
- Accession number :
- 160940094
- Full Text :
- https://doi.org/10.3390/biophysica2040030