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The substitution of a single amino acid with its enantiomer for control over the adjuvant activity of self-assembling peptides

The substitution of a single amino acid with its enantiomer may lead to variations in self-assembled nanostructures and biological functions. In this study, we reported three novel heterochiral peptide hydrogels, Nap-G(D)FFY (gel-1), Nap-GF(D)FY (gel-2) and Nap-GFF(D)Y (gel-3), from Nap-GFFY via the...

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Autores principales: Li, Mingyu, Liu, Mingyuan, Shang, Yuna, Ren, Chunhua, Liu, Jianfeng, Jin, Hongxing, Wang, Zhongyan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9051654/
https://www.ncbi.nlm.nih.gov/pubmed/35493019
http://dx.doi.org/10.1039/c9ra10325b
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author Li, Mingyu
Liu, Mingyuan
Shang, Yuna
Ren, Chunhua
Liu, Jianfeng
Jin, Hongxing
Wang, Zhongyan
author_facet Li, Mingyu
Liu, Mingyuan
Shang, Yuna
Ren, Chunhua
Liu, Jianfeng
Jin, Hongxing
Wang, Zhongyan
author_sort Li, Mingyu
collection PubMed
description The substitution of a single amino acid with its enantiomer may lead to variations in self-assembled nanostructures and biological functions. In this study, we reported three novel heterochiral peptide hydrogels, Nap-G(D)FFY (gel-1), Nap-GF(D)FY (gel-2) and Nap-GFF(D)Y (gel-3), from Nap-GFFY via the substitution of a single amino acid with its enantiomer. We found that the resulting hydrogels possessed diverse self-assembly behaviors and adjuvant activities. Compared to the homochiral l-gel formed from Nap-GFFY, gel-1 was basically similar, gel-2 exhibited a medium improvement in immunocompetence tuning ability, and gel-3 showed the better self-assembly of nanofibers with superior mechanical properties and the ability for slow antigen release. Moreover, the adjuvant effect of gel-3 was prominent, promoting both specific antibody titers and the production of cytokines. Besides, this regulation was more remarkable with respect to enhancing cellular immune responses. Hence, we came to the conclusion in this study that the substitution of a single amino acid with its enantiomer further away from rather than closer to the end-capping group could be important and effective for biofunction regulation. Our study provides a useful strategy for tuning the properties of self-assembling peptides for different biological applications.
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spelling pubmed-90516542022-04-29 The substitution of a single amino acid with its enantiomer for control over the adjuvant activity of self-assembling peptides Li, Mingyu Liu, Mingyuan Shang, Yuna Ren, Chunhua Liu, Jianfeng Jin, Hongxing Wang, Zhongyan RSC Adv Chemistry The substitution of a single amino acid with its enantiomer may lead to variations in self-assembled nanostructures and biological functions. In this study, we reported three novel heterochiral peptide hydrogels, Nap-G(D)FFY (gel-1), Nap-GF(D)FY (gel-2) and Nap-GFF(D)Y (gel-3), from Nap-GFFY via the substitution of a single amino acid with its enantiomer. We found that the resulting hydrogels possessed diverse self-assembly behaviors and adjuvant activities. Compared to the homochiral l-gel formed from Nap-GFFY, gel-1 was basically similar, gel-2 exhibited a medium improvement in immunocompetence tuning ability, and gel-3 showed the better self-assembly of nanofibers with superior mechanical properties and the ability for slow antigen release. Moreover, the adjuvant effect of gel-3 was prominent, promoting both specific antibody titers and the production of cytokines. Besides, this regulation was more remarkable with respect to enhancing cellular immune responses. Hence, we came to the conclusion in this study that the substitution of a single amino acid with its enantiomer further away from rather than closer to the end-capping group could be important and effective for biofunction regulation. Our study provides a useful strategy for tuning the properties of self-assembling peptides for different biological applications. The Royal Society of Chemistry 2020-04-06 /pmc/articles/PMC9051654/ /pubmed/35493019 http://dx.doi.org/10.1039/c9ra10325b Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/
spellingShingle Chemistry
Li, Mingyu
Liu, Mingyuan
Shang, Yuna
Ren, Chunhua
Liu, Jianfeng
Jin, Hongxing
Wang, Zhongyan
The substitution of a single amino acid with its enantiomer for control over the adjuvant activity of self-assembling peptides
title The substitution of a single amino acid with its enantiomer for control over the adjuvant activity of self-assembling peptides
title_full The substitution of a single amino acid with its enantiomer for control over the adjuvant activity of self-assembling peptides
title_fullStr The substitution of a single amino acid with its enantiomer for control over the adjuvant activity of self-assembling peptides
title_full_unstemmed The substitution of a single amino acid with its enantiomer for control over the adjuvant activity of self-assembling peptides
title_short The substitution of a single amino acid with its enantiomer for control over the adjuvant activity of self-assembling peptides
title_sort substitution of a single amino acid with its enantiomer for control over the adjuvant activity of self-assembling peptides
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9051654/
https://www.ncbi.nlm.nih.gov/pubmed/35493019
http://dx.doi.org/10.1039/c9ra10325b
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