Elucidating Bauhinia variegata lectin/phosphatidylcholine interactions in lectin-containing liposomes

Author(s):Show less -

dos Santos, Marinalva Cardoso ^[1] ; Kroetz, Thais ^[2] ; Dora, Cristiana Lima ^[1] ; Giacomelli, Fernando Carlos ^[3] ; Allievi Frizon, Tiago Elias ^[4] ; Pich, Claus Troger ^[4] ; Pinto, Luciano da Silva ^[5] ; Soares, Amanda Sigal ^[5] ; Rodembusch, Fabiano Severo ^[2] ; de Lima, Vania Rodrigues ^[1] ; Dal-Bo, Alexandre Goncalves ^[6]

Affiliation

^[1] Univ Fed Rio Grande FURG, Av Italia Km 8 Campus Carreiros, BR-96201900 Rio Grande, RS - Brazil

^[2] Univ Fed Rio Grande do Sul, Inst Quim, Av Bento Goncalves 9500, BR-91501970 Porto Alegre, RS - Brazil

^[3] Univ Fed ABC, Ctr Ciencias Nat & Humanas, Av Estados 5001, BR-09210580 Santo Andre, SP - Brazil

^[4] Univ Fed Santa Catarina, Campus Ararangua, Rua Pedro Joao Pereira 150, BR-88905120 Ararangua, SC - Brazil

^[5] Univ Fed Pelotas UFPel, Campus Univ S-N, BR-96080705 Pelotas, RS - Brazil

^[6] Univ Extremo Sul Catarinense UNESC, Ave Univ 1105, BR-88806000 Criciuma, SC - Brazil

• Document type: Journal article
• Source: Journal of Colloid and Interface Science; v. 519, p. 232-241, JUN 1 2018.
• Web of Science Citations: 3

Abstract

Investigations focused on the interactions of nanoparticles with lectins are relevant since it is well accepted that such proteins can be recognized by carbohydrates as parts of cell membranes. This can ultimately enhance the cellular uptake of the produced assemblies. In this framework, the physical interactions of phosphatidylcholine (PC) liposomes and the Bauhinia variegate lectin (BVL) are reported here. BVL-liposome interactions were characterized by a variety of techniques to understand the influence of BVL in the structural features, thermodynamic and spectroscopic properties of the hybrid material. The produced system is composed of 56% w/w lectin, and the scattering techniques show the presence of stable vesicular structures with a mean diameter D-H similar to 100 nm. The FTIR and NMR results showed a strong lectin effect on the PC choline region, restricting the rotational motion of the lipid group. The BVL-liposome interaction promoted hardening of the protein as evidenced by circular dichroism spectroscopy. The photophysics results suggest higher rigidity of the system in the presence of BVL. The BVL may be present in the inner or outer polar surface of the liposomes. The system was shown to be relatively stable and therefore potentially useful for carbohydrate recognition of nanoparticles. (C) 2018 Elsevier Inc. All rights reserved. (AU)

• FAPESP's process: 17/00459-4 - Biophysicochemical interactions at the nanobiointerface: the effect of surface features and protein corona on the cellular uptake of polymeric assemblies
• Grantee: Fernando Carlos Giacomelli
• Support Opportunities: Regular Research Grants