Abstract
Supramolecular nanostructures formed through self-assembly can have energy landscapes, which determine their structures and functions depending on the pathways selected for their synthesis and processing and on the conditions they are exposed to after their initial formation. We report here on the structural damage that occurs in supramolecular peptide amphiphile nanostructures, during freezing in aqueous media, and the self-repair pathways that restore their functions. We found that freezing converts long supramolecular nanofibers into shorter ones, compromising their ability to support cell adhesion, but a single heating and cooling cycle reverses the damage and rescues their bioactivity. Thermal energy in this cycle enables noncovalent interactions to reconfigure the nanostructures into the thermodynamically preferred long nanofibers, a repair process that is impeded by kinetic traps. In addition, we found that nanofibers disrupted during freeze-drying also exhibit the ability to undergo thermal self-repair and recovery of their bioactivity, despite the extra disruption caused by the dehydration step. Following both freezing and freeze-drying, which shorten the 1D nanostructures, their self-repair capacity through thermally driven elongation is inhibited by kinetically trapped states, which contain highly stable noncovalent interactions that are difficult to rearrange. These states decrease the extent of thermal nanostructure repair, an observation we hypothesize applies to supramolecular systems in general and is mechanistically linked to suppressed molecular exchange dynamics.
| Original language | English |
|---|---|
| Pages (from-to) | 6832-6841 |
| Number of pages | 10 |
| Journal | Nano Letters |
| Volume | 18 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - Nov 14 2018 |
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Keywords
- biomaterials
- cell-nanostructure interactions
- regenerative medicine
- self-assembly
- self-repair
- Supramolecular nanostructures
ASJC Scopus subject areas
- Bioengineering
- Chemistry(all)
- Materials Science(all)
- Condensed Matter Physics
- Mechanical Engineering
Cite this
Self-Repair of Structure and Bioactivity in a Supramolecular Nanostructure. / Chen, Charlotte H.; Palmer, Liam C.; Stupp, Samuel I.
In: Nano Letters, Vol. 18, No. 11, 14.11.2018, p. 6832-6841.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Self-Repair of Structure and Bioactivity in a Supramolecular Nanostructure
AU - Chen, Charlotte H.
AU - Palmer, Liam C.
AU - Stupp, Samuel I
PY - 2018/11/14
Y1 - 2018/11/14
N2 - Supramolecular nanostructures formed through self-assembly can have energy landscapes, which determine their structures and functions depending on the pathways selected for their synthesis and processing and on the conditions they are exposed to after their initial formation. We report here on the structural damage that occurs in supramolecular peptide amphiphile nanostructures, during freezing in aqueous media, and the self-repair pathways that restore their functions. We found that freezing converts long supramolecular nanofibers into shorter ones, compromising their ability to support cell adhesion, but a single heating and cooling cycle reverses the damage and rescues their bioactivity. Thermal energy in this cycle enables noncovalent interactions to reconfigure the nanostructures into the thermodynamically preferred long nanofibers, a repair process that is impeded by kinetic traps. In addition, we found that nanofibers disrupted during freeze-drying also exhibit the ability to undergo thermal self-repair and recovery of their bioactivity, despite the extra disruption caused by the dehydration step. Following both freezing and freeze-drying, which shorten the 1D nanostructures, their self-repair capacity through thermally driven elongation is inhibited by kinetically trapped states, which contain highly stable noncovalent interactions that are difficult to rearrange. These states decrease the extent of thermal nanostructure repair, an observation we hypothesize applies to supramolecular systems in general and is mechanistically linked to suppressed molecular exchange dynamics.
AB - Supramolecular nanostructures formed through self-assembly can have energy landscapes, which determine their structures and functions depending on the pathways selected for their synthesis and processing and on the conditions they are exposed to after their initial formation. We report here on the structural damage that occurs in supramolecular peptide amphiphile nanostructures, during freezing in aqueous media, and the self-repair pathways that restore their functions. We found that freezing converts long supramolecular nanofibers into shorter ones, compromising their ability to support cell adhesion, but a single heating and cooling cycle reverses the damage and rescues their bioactivity. Thermal energy in this cycle enables noncovalent interactions to reconfigure the nanostructures into the thermodynamically preferred long nanofibers, a repair process that is impeded by kinetic traps. In addition, we found that nanofibers disrupted during freeze-drying also exhibit the ability to undergo thermal self-repair and recovery of their bioactivity, despite the extra disruption caused by the dehydration step. Following both freezing and freeze-drying, which shorten the 1D nanostructures, their self-repair capacity through thermally driven elongation is inhibited by kinetically trapped states, which contain highly stable noncovalent interactions that are difficult to rearrange. These states decrease the extent of thermal nanostructure repair, an observation we hypothesize applies to supramolecular systems in general and is mechanistically linked to suppressed molecular exchange dynamics.
KW - biomaterials
KW - cell-nanostructure interactions
KW - regenerative medicine
KW - self-assembly
KW - self-repair
KW - Supramolecular nanostructures
UR - http://www.scopus.com/inward/record.url?scp=85056281121&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85056281121&partnerID=8YFLogxK
U2 - 10.1021/acs.nanolett.8b02709
DO - 10.1021/acs.nanolett.8b02709
M3 - Article
VL - 18
SP - 6832
EP - 6841
JO - Nano Letters
JF - Nano Letters
SN - 1530-6984
IS - 11
ER -