Systematic Moiety Variations of Ultrashort Peptides Produce Profound Effects on Self-Assembly, Nanostructure Formation, Hydrogelation, and Phase Transition

Handle URI:
http://hdl.handle.net/10754/625920
Title:
Systematic Moiety Variations of Ultrashort Peptides Produce Profound Effects on Self-Assembly, Nanostructure Formation, Hydrogelation, and Phase Transition
Authors:
Chan, Kiat Hwa; Xue, Bo; Robinson, Robert C.; Hauser, Charlotte ( 0000-0001-8251-7246 )
Abstract:
Self-assembly of small biomolecules is a prevalent phenomenon that is increasingly being recognised to hold the key to building complex structures from simple monomeric units. Small peptides, in particular ultrashort peptides containing up to seven amino acids, for which our laboratory has found many biomedical applications, exhibit immense potential in this regard. For next-generation applications, more intricate control is required over the self-assembly processes. We seek to find out how subtle moiety variation of peptides can affect self-assembly and nanostructure formation. To this end, we have selected a library of 54 tripeptides, derived from systematic moiety variations from seven tripeptides. Our study reveals that subtle structural changes in the tripeptides can exert profound effects on self-assembly, nanostructure formation, hydrogelation, and even phase transition of peptide nanostructures. By comparing the X-ray crystal structures of two tripeptides, acetylated leucine-leucine-glutamic acid (Ac-LLE) and acetylated tyrosine-leucine-aspartic acid (Ac-YLD), we obtained valuable insights into the structural factors that can influence the formation of supramolecular peptide structures. We believe that our results have major implications on the understanding of the factors that affect peptide self-assembly. In addition, our findings can potentially assist current computational efforts to predict and design self-assembling peptide systems for diverse biomedical applications.
KAUST Department:
Laboratory for Nanomedicine, King Abdullah University of Science and Technology, Thuwal, 23955-6900, Saudi Arabia.
Citation:
Chan KH, Xue B, Robinson RC, Hauser CAE (2017) Systematic Moiety Variations of Ultrashort Peptides Produce Profound Effects on Self-Assembly, Nanostructure Formation, Hydrogelation, and Phase Transition. Scientific Reports 7. Available: http://dx.doi.org/10.1038/s41598-017-12694-9.
Publisher:
Springer Nature
Journal:
Scientific Reports
Issue Date:
4-Oct-2017
DOI:
10.1038/s41598-017-12694-9
Type:
Article
ISSN:
2045-2322
Sponsors:
This work is funded by the Agency for Science, Technology and Research (A*STAR), Singapore.
Additional Links:
https://www.nature.com/articles/s41598-017-12694-9
Appears in Collections:
Articles

Full metadata record

DC FieldValue Language
dc.contributor.authorChan, Kiat Hwaen
dc.contributor.authorXue, Boen
dc.contributor.authorRobinson, Robert C.en
dc.contributor.authorHauser, Charlotteen
dc.date.accessioned2017-10-22T11:48:14Z-
dc.date.available2017-10-22T11:48:14Z-
dc.date.issued2017-10-04en
dc.identifier.citationChan KH, Xue B, Robinson RC, Hauser CAE (2017) Systematic Moiety Variations of Ultrashort Peptides Produce Profound Effects on Self-Assembly, Nanostructure Formation, Hydrogelation, and Phase Transition. Scientific Reports 7. Available: http://dx.doi.org/10.1038/s41598-017-12694-9.en
dc.identifier.issn2045-2322en
dc.identifier.doi10.1038/s41598-017-12694-9en
dc.identifier.urihttp://hdl.handle.net/10754/625920-
dc.description.abstractSelf-assembly of small biomolecules is a prevalent phenomenon that is increasingly being recognised to hold the key to building complex structures from simple monomeric units. Small peptides, in particular ultrashort peptides containing up to seven amino acids, for which our laboratory has found many biomedical applications, exhibit immense potential in this regard. For next-generation applications, more intricate control is required over the self-assembly processes. We seek to find out how subtle moiety variation of peptides can affect self-assembly and nanostructure formation. To this end, we have selected a library of 54 tripeptides, derived from systematic moiety variations from seven tripeptides. Our study reveals that subtle structural changes in the tripeptides can exert profound effects on self-assembly, nanostructure formation, hydrogelation, and even phase transition of peptide nanostructures. By comparing the X-ray crystal structures of two tripeptides, acetylated leucine-leucine-glutamic acid (Ac-LLE) and acetylated tyrosine-leucine-aspartic acid (Ac-YLD), we obtained valuable insights into the structural factors that can influence the formation of supramolecular peptide structures. We believe that our results have major implications on the understanding of the factors that affect peptide self-assembly. In addition, our findings can potentially assist current computational efforts to predict and design self-assembling peptide systems for diverse biomedical applications.en
dc.description.sponsorshipThis work is funded by the Agency for Science, Technology and Research (A*STAR), Singapore.en
dc.publisherSpringer Natureen
dc.relation.urlhttps://www.nature.com/articles/s41598-017-12694-9en
dc.rightsThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.en
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.titleSystematic Moiety Variations of Ultrashort Peptides Produce Profound Effects on Self-Assembly, Nanostructure Formation, Hydrogelation, and Phase Transitionen
dc.typeArticleen
dc.contributor.departmentLaboratory for Nanomedicine, King Abdullah University of Science and Technology, Thuwal, 23955-6900, Saudi Arabia.en
dc.identifier.journalScientific Reportsen
dc.eprint.versionPublisher's Version/PDFen
dc.contributor.institutionDivision of Science, Yale-NUS College, 16 College Avenue West, Singapore, 138527, Singapore.en
dc.contributor.institutionInstitute of Bioengineering and Nanotechnology, Biopolis, A*STAR (Agency for Science, Technology and Research), Singapore, 138669, Singaporeen
dc.contributor.institutionDepartment of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, 8 Medical Drive, Singapore, 117597, Singapore.en
dc.contributor.institutionNUS Synthetic Biology for Clinical and Technological Innovation, Centre for Life Sciences, National University of Singapore, 28 Medical Drive, Singapore, 117456, Singaporeen
dc.contributor.institutionInstitute of Molecular and Cell Biology, Biopolis, A*STAR (Agency for Science, Technology and Research), Singapore, 138673, Singaporeen
dc.contributor.institutionResearch Institute for Interdisciplinary Science, Okayama University, Okayama, 700-8530, Japan.en
kaust.authorHauser, Charlotteen
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