Self-Repair of Structure and Bioactivity in a Supramolecular Nanostructure

Charlotte H. Chen, Liam C. Palmer, Samuel I Stupp

Research output: Contribution to journalArticle

1 Citation (Scopus)

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 languageEnglish
Pages (from-to)6832-6841
Number of pages10
JournalNano Letters
Volume18
Issue number11
DOIs
Publication statusPublished - Nov 14 2018

Fingerprint

Bioactivity
freezing
Nanostructures
freeze drying
Repair
Nanofibers
Freezing
damage
cycles
Drying
thermal energy
dehydration
elongation
peptides
self assembly
adhesion
recovery
Amphiphiles
traps
interactions

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 journalArticle

Chen, Charlotte H. ; Palmer, Liam C. ; Stupp, Samuel I. / Self-Repair of Structure and Bioactivity in a Supramolecular Nanostructure. In: Nano Letters. 2018 ; Vol. 18, No. 11. pp. 6832-6841.
@article{48772e9d16db44aa812872dd2006224b,
title = "Self-Repair of Structure and Bioactivity in a Supramolecular Nanostructure",
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.",
keywords = "biomaterials, cell-nanostructure interactions, regenerative medicine, self-assembly, self-repair, Supramolecular nanostructures",
author = "Chen, {Charlotte H.} and Palmer, {Liam C.} and Stupp, {Samuel I}",
year = "2018",
month = "11",
day = "14",
doi = "10.1021/acs.nanolett.8b02709",
language = "English",
volume = "18",
pages = "6832--6841",
journal = "Nano Letters",
issn = "1530-6984",
publisher = "American Chemical Society",
number = "11",

}

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

C2 - 30379077

AN - SCOPUS:85056281121

VL - 18

SP - 6832

EP - 6841

JO - Nano Letters

JF - Nano Letters

SN - 1530-6984

IS - 11

ER -