Title of the paper: 

Enhancing the Magnitude of Antibody Responses through Biomaterial Stereochemistry

 

Authors: 

Rajagopal AppavuCharles B. ChessonAlexey Y. KoyfmanJoshua D. SnookFrederick J. KohlhappAndrew Zloza, and Jai S. Rudra

 

 

University/Institute: 

The University of Texas Medical Branch, Galveston, Texas 77555, United States


 

Abstracts (or short description):

d-Amino acid analogs of peptides and proteins are attractive for applications in biotechnology and medicine due to their reduced proteolytic sensitivity. Here, we report that self-assembling peptide nanofibers composed of d-amino acids act as immune adjuvants, and investigate their ability to induce antibody responses in comparison to their l-amino acid counterparts. The model antigenic peptide OVA (chicken egg ovalbumin aa 323–339) from chicken egg ovalbumin, known to elicit antibody responses in mice, was linked to an l- or d-amino acid self-assembling peptide domain to generate enantiomeric nanofibers displaying the same epitope. The chiral nature of the fusion peptides was confirmed by circular dichrosim spectroscopy and transmission electron microscopy studies indicated that OVA-bearing enantiomers self-assembled into nanofibers with similar morphologies. In mice, d-amino acid peptide nanofibers displaying OVA elicited stronger antibody responses, equivalent levels of CD4+ T cell responses, and long-term antigen-presentation in vivo compared to l-amino acid nanofibers. Our findings indicate that self-assembling peptides composed of d-amino acids are strong immune adjuvants and that biomaterial stereochemistry can be used as a design tool to program adaptive immune responses for vaccine development.

 

Journal, Issue, Page Nr.:

ACS Biomater. Sci. Eng., Article ASAP

DOI: 10.1021/acsbiomaterials.5b00139

 

Links to the paper (link to the journal webpage):

http://pubs.acs.org/doi/abs/10.1021/acsbiomaterials.5b00139

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