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231226s2022 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.2c02179
|2 doi
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|a pubmed24n1153.xml
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|a (DE-627)NLM346188067
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|a (NLM)36101985
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|a DE-627
|b ger
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|e rakwb
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|a eng
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| 100 |
1 |
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|a Sato, Ai
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Thermodynamics for the Self-Assembly of Alkylated Peptides
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|c 2022
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|a Text
|b txt
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|a ƒaComputermedien
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|a ƒa Online-Ressource
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|a Date Completed 28.09.2022
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|a Date Revised 13.10.2022
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Self-assembling peptides form aggregates with various nanostructures such as spheres, sheets, and fibers and have potential applications in nanomedicine and drug delivery. The alkylation of peptides is a promising strategy for controlling the self-assembly of peptides. In this study, we investigated the thermodynamic properties associated with the aggregation of alkyl-chain-modified self-assembling peptides. The tripeptide sequence, KYF, which has been reported to form fibrous aggregates via self-assembly, was modified with various fatty acids at the N-terminus. The fibrous morphology of the aggregates was observed by transmission electron microscopy and atomic force microscopy. Thioflavin T fluorescence and circular dichroism spectroscopy revealed the formation of β-sheet structures. The critical micelle concentration and its temperature dependence were determined to obtain the thermodynamic parameters for aggregation. The results showed that the aggregation was an entropy-driven process at low temperatures, whereas it was enthalpy-driven at high temperatures. The negative heat capacity changes for aggregation suggested that hydrophobic interactions were the major driving force for self-assembly. Other entropic and enthalpic interactions were also contributed in part to the self-assembly. We individually identified the contributions of the peptide and alkyl chain moiety to the self-assembly. These contributions can be explained by the theoretical values for the self-assembly of each component. The results of this study provide fundamental insights into the design of self-associating peptides
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Fatty Acids
|2 NLM
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|a Micelles
|2 NLM
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| 650 |
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|a Peptides
|2 NLM
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|a Ikeda, Keisuke
|e verfasserin
|4 aut
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1 |
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|a Nakao, Hiroyuki
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Nakano, Minoru
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 38(2022), 38 vom: 27. Sept., Seite 11801-11809
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
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|g volume:38
|g year:2022
|g number:38
|g day:27
|g month:09
|g pages:11801-11809
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|u http://dx.doi.org/10.1021/acs.langmuir.2c02179
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