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Article: Nanoscale Multiparametric Imaging of Peptide-Assembled Nanofibrillar Hydrogels by Atomic Force Microscopy

TitleNanoscale Multiparametric Imaging of Peptide-Assembled Nanofibrillar Hydrogels by Atomic Force Microscopy
Authors
KeywordsForce
Imaging
Self-assembly
Peptides
Electron tubes
Issue Date2019
PublisherIEEE. The Journal's web site is located at http://ieeexplore.ieee.org/xpl/RecentIssue.jsp?punumber=7729
Citation
IEEE Transactions on Nanotechnology, 2019, v. 18, p. 315-328 How to Cite?
AbstractPeptide-assembled hydrogels have emerged as a promising biomaterial for tissue engineering due to their controllable structures as well as biocompatible and biodegradable characteristics. However, the detailed situations of nanofibrillar mechanics during the formation of peptide-assembled hydrogels remain poorly understood. The advent of atomic force microscopy (AFM) provides a powerful tool for nanoscale characterizations and measurements of native biomaterials without pretreatments. In this paper, AFM peak force tapping multiparametric imaging was utilized to investigate the morphology and mechanics of individual nanofibrils during the gelation and degradation process of peptide-assembly hydrogels. Nanofibrillar hydrogels were fabricated by the self-assembly reactions of phenylalanine peptide molecules. AFM topography imaging distinctly visualized the diverse assembly behaviors of peptide-formed nanofibrils during the gelation and degradation of hydrogels, which were significantly correlated with the changes of nanofibrillar mechanics (Young's modulus, adhesion force, deformation, and persistence length) revealed by AFM mechanical imaging. The research provides a novel idea for nanoscale imaging and mechanical analysis of nanofibrillar behaviors in peptide-assembled hydrogels, which will have potential impacts on the characterization and design of supramolecular biomaterials.
Persistent Identifierhttp://hdl.handle.net/10722/282926
ISSN
2020 Impact Factor: 2.57
2020 SCImago Journal Rankings: 0.574
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLI, M-
dc.contributor.authorXi, N-
dc.contributor.authorWANG, Y-
dc.contributor.authorLIU, L-
dc.date.accessioned2020-06-05T06:23:08Z-
dc.date.available2020-06-05T06:23:08Z-
dc.date.issued2019-
dc.identifier.citationIEEE Transactions on Nanotechnology, 2019, v. 18, p. 315-328-
dc.identifier.issn1536-125X-
dc.identifier.urihttp://hdl.handle.net/10722/282926-
dc.description.abstractPeptide-assembled hydrogels have emerged as a promising biomaterial for tissue engineering due to their controllable structures as well as biocompatible and biodegradable characteristics. However, the detailed situations of nanofibrillar mechanics during the formation of peptide-assembled hydrogels remain poorly understood. The advent of atomic force microscopy (AFM) provides a powerful tool for nanoscale characterizations and measurements of native biomaterials without pretreatments. In this paper, AFM peak force tapping multiparametric imaging was utilized to investigate the morphology and mechanics of individual nanofibrils during the gelation and degradation process of peptide-assembly hydrogels. Nanofibrillar hydrogels were fabricated by the self-assembly reactions of phenylalanine peptide molecules. AFM topography imaging distinctly visualized the diverse assembly behaviors of peptide-formed nanofibrils during the gelation and degradation of hydrogels, which were significantly correlated with the changes of nanofibrillar mechanics (Young's modulus, adhesion force, deformation, and persistence length) revealed by AFM mechanical imaging. The research provides a novel idea for nanoscale imaging and mechanical analysis of nanofibrillar behaviors in peptide-assembled hydrogels, which will have potential impacts on the characterization and design of supramolecular biomaterials.-
dc.languageeng-
dc.publisherIEEE. The Journal's web site is located at http://ieeexplore.ieee.org/xpl/RecentIssue.jsp?punumber=7729-
dc.relation.ispartofIEEE Transactions on Nanotechnology-
dc.rightsIEEE Transactions on Nanotechnology. Copyright © IEEE.-
dc.rights©20xx IEEE. Personal use of this material is permitted. Permission from IEEE must be obtained for all other uses, in any current or future media, including reprinting/republishing this material for advertising or promotional purposes, creating new collective works, for resale or redistribution to servers or lists, or reuse of any copyrighted component of this work in other works.-
dc.subjectForce-
dc.subjectImaging-
dc.subjectSelf-assembly-
dc.subjectPeptides-
dc.subjectElectron tubes-
dc.titleNanoscale Multiparametric Imaging of Peptide-Assembled Nanofibrillar Hydrogels by Atomic Force Microscopy-
dc.typeArticle-
dc.identifier.emailXi, N: xining@hku.hk-
dc.identifier.authorityXi, N=rp02044-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1109/TNANO.2019.2904583-
dc.identifier.scopuseid_2-s2.0-85063811553-
dc.identifier.hkuros310090-
dc.identifier.volume18-
dc.identifier.spage315-
dc.identifier.epage328-
dc.identifier.isiWOS:000463063500003-
dc.publisher.placeUnited States-
dc.identifier.issnl1536-125X-

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