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On the Mechanism of...
On the Mechanism of Self-Assembly by a Hydrogel-Forming Peptide
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- Braun, Gabriel A. (author)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,Haverford College
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- Ary, Beatrice E. (author)
- Haverford College
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- Dear, Alexander J. (author)
- Harvard University,University of Cambridge
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- Rohn, Matthew C.H. (author)
- Haverford College
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- Payson, Abigail M. (author)
- Haverford College
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- Lee, David S.M. (author)
- Haverford College
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- Parry, Robert C. (author)
- Haverford College
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- Friedman, Connie (author)
- Haverford College
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- Knowles, Tuomas P.J. (author)
- University of Cambridge
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- Linse, Sara (author)
- Lund University,Lunds universitet,NanoLund: Centre for Nanoscience,Annan verksamhet, LTH,Lunds Tekniska Högskola,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Other operations, LTH,Faculty of Engineering, LTH,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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- Åkerfeldt, Karin S. (author)
- Haverford College
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(creator_code:org_t)
- 2020-11-10
- 2020
- English 14 s.
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In: Biomacromolecules. - : American Chemical Society (ACS). - 1525-7797 .- 1526-4602. ; 21:12, s. 4781-4794
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http://dx.doi.org/10...
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Abstract
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
- NATURVETENSKAP -- Kemi -- Polymerkemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Polymer Chemistry (hsv//eng)
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- By the author/editor
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Braun, Gabriel A ...
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Ary, Beatrice E.
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Dear, Alexander ...
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Rohn, Matthew C. ...
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Payson, Abigail ...
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Lee, David S.M.
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show more...
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Parry, Robert C.
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Friedman, Connie
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Knowles, Tuomas ...
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Linse, Sara
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Åkerfeldt, Karin ...
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- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biochemistry and ...
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Chemical Science ...
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and Polymer Chemistr ...
- Articles in the publication
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Biomacromolecule ...
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Lund University