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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.)

FTIR study of secondary structure changes in Epidermal Growth Factor by gold nanoparticle conjugation

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Author(s):
Bhattacharjee, T. T. [1] ; Castilho, M. L. [2] ; de Oliveira, I. R. [3] ; Jesus, V. P. S. [2] ; Hewitt, K. C. [4] ; Raniero, L. [1]
Total Authors: 6
Affiliation:
[1] Univ Vale Paraiba, Inst Pesquisa & Desenvolvimento, Lab Nanossensores, Av Shishima Hifumi 2911, BR-12244000 Sao Jose Dos Campos, SP - Brazil
[2] Univ Vale Paraiba, Inst Pesquisa & Desenvolvimento, Lab Bionanotecnol, Av Shishima Hifumi 2911, BR-12244000 Sao Jose Dos Campos, SP - Brazil
[3] Univ Vale Paraiba, Inst Pesquisa & Desenvolvimento, Lab Ceram Avancadas, Av Shishima Hifumi 2911, BR-12244000 Sao Jose Dos Campos, SP - Brazil
[4] Dalhousie Univ, Dept Phys & Atmospher Sci, 6310 Coburg Rd, Halifax, NS B3H 4R2 - Canada
Total Affiliations: 4
Document type: Journal article
Source: BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS; v. 1862, n. 3, p. 495-500, MAR 2018.
Web of Science Citations: 2
Abstract

Conformation of protein is vital to its function, but may get affected when processing to manufacture products. It is therefore important to understand structural changes during each step of production. In this study, we investigate secondary structure changes in the targeting protein Epidermal Growth Factor (EGF) during synthesis of theranostic bifunctional nanoparticle, devised for Photodynamic therapy of breast cancer. We acquired FTIR spectra of EGF; unconjugated, post treatment with alpha-lipoic acid, attached to gold nanoparticle, and bound to the bifunctional nanoprobe. We observed decreasing disordered structures and turns, and increasing loops, as the synthesis process progressed. There was an overall increase in beta-sheets in final product compared to pure EGF, but this increase was not linear and fluctuated. Previous crystal structure studies on EGF-EGFR complex have shown loops and beta-sheets to be important in the binding interaction. Since our study found increase in these structures in the final product, no adverse effect on binding function of EGF was expected. This was confirmed by functional assays. Such studies may help modify synthesis procedures, and thus secondary structures of proteins, enabling increased functionality and optimum results. (AU)

FAPESP's process: 13/17404-7 - Photodynamic therapy associated with nanoprobes for treating cancer
Grantee:Leandro José Raniero
Support type: Regular Research Grants