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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

The lipid composition affects Trastuzumab adsorption at monolayers at the air-water interface

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Author(s):
Sakai, Andrei [1] ; de Sousa Mesquista, Ana Paula [2] ; Nader, Helena B. [1] ; Lopes, Carla Cristina [1] ; Nakanishi, Waka [3, 4] ; Ariga, Katsuhiko [5, 3] ; Caseli, Luciano [1]
Total Authors: 7
Affiliation:
[1] Univ Fed Sao Paulo, Inst Environm Chem & Pharmaceut Sci, Diadema, SP - Brazil
[2] Univ Fed Sao Paulo, Dept Mol Biol, Sao Paulo, SP - Brazil
[3] Natl Inst Mat Sci, Int Ctr Mat Nanoarchitecton WPI MANA, 1-1 Namiki, Tsukuba, Ibaraki 3050044 - Japan
[4] Natl Inst Mat Sci, Res Ctr Funct Mat, 1-2-1 Sengen, Tsukuba, Ibaraki 3050047 - Japan
[5] Univ Tokyo, Grad Sch Frontier Sci, Dept Adv Mat Sci, 5-1-5 Kashiwanoha, Kashiwa, Chiba 2778561 - Japan
Total Affiliations: 5
Document type: Journal article
Source: Chemistry and Physics of Lipids; v. 227, MAR 2020.
Web of Science Citations: 0
Abstract

Trastuzumab (Tmab), an antibody for breast cancer, was incorporated in Langmuir monolayers with different lipidic compositions to investigate the drug action in lipidic interfaces of pharmaceutical interest. Tmab caused all lipid films to expand as confirmed with by surface pressure-area isotherm, proving its incorporation. It also affected the compressional and structural properties as observed by in-plane elasticity curves and polarization modulation reflection-absorption infrared spectroscopy (PM-IRRAS), respectively. Although Tmab did not change significantly the compressional modulus for dipalmitoylphosphatidylcholine (DPPC) monolayers, it decreased it for the mixtures of DPPC with cholesterol. In contrast, for dipalmitoylphosphoethanolamine (DPPE), Tmab increased the compressional modulus for both monolayers, pure DPPE or mixed with cholesterol. While Brewster Angle Microscopy showed discrete distinctive morphological patterns for the monolayers investigated, PM-IRRAS showed that Tmab caused an increased number of gauche conformers related to the CH2 stretching mode for the lipid acyl chains, suggesting molecular disorder. Furthermore, the antibody kept the (beta-sheet structure of the polypeptide backbone adsorbed at the lipid monolayers although the secondary conformation altered according to the film composition at the air-water interface. As a result, the results suggest that the membrane lipid profile affects the adsorption of Tmab at lipid monolayers, which can be important for the incorporation of this drug in lipidic supramolecular systems like in liposomes for drug delivery and in bio-membranes. (AU)

FAPESP's process: 19/03239-0 - Nanostructured interfaces for the investigation of bioactive substances in cell membrane models and for the construction of optoelectronic devices
Grantee:Luciano Caseli
Support Opportunities: Regular Research Grants