TY - JOUR
T1 - Dynamics of encapsulated hepatitis B surface antigen
T2 - A combined neutron spectroscopy and thermo-analysis study
AU - Rasmussen, Martin K.
AU - Pereira, José E.M.
AU - Berg, Marcella C.
AU - Iles, Gail N.
AU - de Souza, Nicolas R.
AU - Jalarvo, Niina H.
AU - Botosso, Viviane F.
AU - Sant’Anna, Osvaldo A.
AU - Fantini, Marcia C.A.
AU - Bordallo, Heloisa N.
PY - 2019/3/1
Y1 - 2019/3/1
N2 - As a consequence of its ordered pore architecture, mesoporous SBA-15 offers new possibilities for incorporating biological agents. Considering its applicability in oral vaccination, which shows more beneficial features when compared with parenteral vaccines, SBA-15 is also seen as a very promising adjuvant to carry, protect, and deliver entrapped antigens. Recent studies have shown several remarkable features in the immunization of hepatitis B, a viral disease transmitted mainly through blood or serum transfer. However, the surface antigen of the hepatitis B virus, HBsAg, is too large to fit inside the SBA-15 matrix with mean pore diameter around 10 nm, thus raising the question of how SBA-15 can protect the antigen. In this work, thermal analysis combined with neutron spectroscopy allowed us to shed light on the interactions between HBsAg and SBA-15 as well as on the role that these interactions play in the efficiency of this promising oral vaccination method. This information was obtained by verifying how the dynamic behaviour of the antigen is modified under confinement in SBA-15, thus also establishing an experimental method for verifying molecular dynamics simulations.
AB - As a consequence of its ordered pore architecture, mesoporous SBA-15 offers new possibilities for incorporating biological agents. Considering its applicability in oral vaccination, which shows more beneficial features when compared with parenteral vaccines, SBA-15 is also seen as a very promising adjuvant to carry, protect, and deliver entrapped antigens. Recent studies have shown several remarkable features in the immunization of hepatitis B, a viral disease transmitted mainly through blood or serum transfer. However, the surface antigen of the hepatitis B virus, HBsAg, is too large to fit inside the SBA-15 matrix with mean pore diameter around 10 nm, thus raising the question of how SBA-15 can protect the antigen. In this work, thermal analysis combined with neutron spectroscopy allowed us to shed light on the interactions between HBsAg and SBA-15 as well as on the role that these interactions play in the efficiency of this promising oral vaccination method. This information was obtained by verifying how the dynamic behaviour of the antigen is modified under confinement in SBA-15, thus also establishing an experimental method for verifying molecular dynamics simulations.
UR - http://www.scopus.com/inward/record.url?scp=85063460371&partnerID=8YFLogxK
U2 - 10.1140/epjst/e2019-700103-x
DO - 10.1140/epjst/e2019-700103-x
M3 - Journal article
AN - SCOPUS:85063460371
SN - 1951-6355
VL - 227
SP - 2393
EP - 2399
JO - European Physical Journal. Special Topics
JF - European Physical Journal. Special Topics
IS - 17
ER -
