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On the Mechanism of Self-Assembly by a Hydrogel-Forming Peptide

Braun, Gabriel A. LU ; Ary, Beatrice E. ; Dear, Alexander J. ; Rohn, Matthew C.H. ; Payson, Abigail M. ; Lee, David S.M. ; Parry, Robert C. ; Friedman, Connie ; Knowles, Tuomas P.J. and Linse, Sara LU , et al. (2020) In Biomacromolecules 21(12). p.4781-4794
Abstract

Self-assembling peptide-based hydrogels are a class of tunable soft materials that have been shown to be highly useful for a number of biomedical applications. The dynamic formation of the supramolecular fibrils that compose these materials has heretofore remained poorly characterized. A better understanding of this process would provide important insights into the behavior of these systems and could aid in the rational design of new peptide hydrogels. Here, we report the determination of the microscopic steps that underpin the self-assembly of a hydrogel-forming peptide, SgI37-49. Using theoretical models of linear polymerization to analyze the kinetic self-assembly data, we show that SgI37-49 fibril formation is driven by... (More)

Self-assembling peptide-based hydrogels are a class of tunable soft materials that have been shown to be highly useful for a number of biomedical applications. The dynamic formation of the supramolecular fibrils that compose these materials has heretofore remained poorly characterized. A better understanding of this process would provide important insights into the behavior of these systems and could aid in the rational design of new peptide hydrogels. Here, we report the determination of the microscopic steps that underpin the self-assembly of a hydrogel-forming peptide, SgI37-49. Using theoretical models of linear polymerization to analyze the kinetic self-assembly data, we show that SgI37-49 fibril formation is driven by fibril-catalyzed secondary nucleation and that all the microscopic processes involved in SgI37-49 self-assembly display an enzyme-like saturation behavior. Moreover, this analysis allows us to quantify the rates of the underlying processes at different peptide concentrations and to calculate the time evolution of these reaction rates over the time course of self-assembly. We demonstrate here a new mechanistic approach for the study of self-assembling hydrogel-forming peptides, which is complementary to commonly used materials science characterization techniques.

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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biomacromolecules
volume
21
issue
12
pages
14 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • scopus:85096575940
  • pmid:33170649
ISSN
1525-7797
DOI
10.1021/acs.biomac.0c00989
language
English
LU publication?
yes
id
81c9ce61-6f46-4d08-bb94-1c402421ff09
date added to LUP
2020-12-09 07:51:17
date last changed
2021-05-16 05:22:59
@article{81c9ce61-6f46-4d08-bb94-1c402421ff09,
  abstract     = {<p>Self-assembling peptide-based hydrogels are a class of tunable soft materials that have been shown to be highly useful for a number of biomedical applications. The dynamic formation of the supramolecular fibrils that compose these materials has heretofore remained poorly characterized. A better understanding of this process would provide important insights into the behavior of these systems and could aid in the rational design of new peptide hydrogels. Here, we report the determination of the microscopic steps that underpin the self-assembly of a hydrogel-forming peptide, SgI37-49. Using theoretical models of linear polymerization to analyze the kinetic self-assembly data, we show that SgI37-49 fibril formation is driven by fibril-catalyzed secondary nucleation and that all the microscopic processes involved in SgI37-49 self-assembly display an enzyme-like saturation behavior. Moreover, this analysis allows us to quantify the rates of the underlying processes at different peptide concentrations and to calculate the time evolution of these reaction rates over the time course of self-assembly. We demonstrate here a new mechanistic approach for the study of self-assembling hydrogel-forming peptides, which is complementary to commonly used materials science characterization techniques.</p>},
  author       = {Braun, Gabriel A. and Ary, Beatrice E. and Dear, Alexander J. and Rohn, Matthew C.H. and Payson, Abigail M. and Lee, David S.M. and Parry, Robert C. and Friedman, Connie and Knowles, Tuomas P.J. and Linse, Sara and Åkerfeldt, Karin S.},
  issn         = {1525-7797},
  language     = {eng},
  month        = {12},
  number       = {12},
  pages        = {4781--4794},
  publisher    = {The American Chemical Society (ACS)},
  series       = {Biomacromolecules},
  title        = {On the Mechanism of Self-Assembly by a Hydrogel-Forming Peptide},
  url          = {http://dx.doi.org/10.1021/acs.biomac.0c00989},
  doi          = {10.1021/acs.biomac.0c00989},
  volume       = {21},
  year         = {2020},
}