Enzyme-Catalyzed Formation of Supramolecular Hydrogels as Promising Vaccine Adjuvants

Promising vaccine adjuvants of self‐assembling peptide hydrogels for protein ovalbumin (OVA) are introduced in this study. The hydrogels are formed by the enzyme of phosphatase, and the vaccine adjuvant potency of both l‐ and d‐peptide hydrogels is evaluated. The results indicate that, compared with...

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Bibliographic Details
Published in:Advanced functional materials 2016-03, Vol.26 (11), p.1822-1829
Main Authors: Wang, Huaimin, Luo, Zichao, Wang, Youzhi, He, Tao, Yang, Chengbiao, Ren, Chunhua, Ma, Linsha, Gong, Changyang, Li, Xingyi, Yang, Zhimou
Format: Article
Language:English
Subjects:
adjuvant
Adjuvants
Antigens
Formations
Hydrogels
Lymph
Peptides
Proteins
self-assembly
supramolecular hydrogel
vaccine
Vaccines
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Summary:Promising vaccine adjuvants of self‐assembling peptide hydrogels for protein ovalbumin (OVA) are introduced in this study. The hydrogels are formed by the enzyme of phosphatase, and the vaccine adjuvant potency of both l‐ and d‐peptide hydrogels is evaluated. The results indicate that, compared with the clinically used alum adjuvant, both l‐ and d‐peptide hydrogels can increase the IgG production of OVA for about 1.3 and 3.8 times, respectively. Both gels can enhance antigen uptake and induce dendritic cell maturation, and promote and prolong accumulation of antigen in lymph node, as well as evoke germinal center formation. However, the d‐peptide hydrogel with OVA exhibits a slightly more efficient accumulation of OVA in the lymph nodes and seems preventing tumor growth more significantly than its l‐counterpart. With the good biocompatibility and degradability of peptide hydrogels, the hydrogels described in this study have big potential for the production of protein vaccines for immunotherapy against different diseases. Short peptides and the protein antigen can coassemble into supramolecular hydrogels capable of raising both humoral and cellular immune responses in mice.
ISSN:1616-301X
1616-3028
DOI:10.1002/adfm.201505188