gamma-Zein secondary structure in solution by circular dichroism |
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| Authors: | Bicudo Tatiana C Bicudo Rogério C Forato Lucimara A Beltramini Leila M Batista Luiz A R Filho Rubens Bernardes Colnago Luiz A |
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| Institution: | 1. Universidade de S?o Paulo, Instituto de Química de S?o Carlos, Av. Trabalhador S?ocarlense, 400, S?o Carlos, SP 13560‐970, Brazil;2. Universidade Federal da Paraíba, Departamento de Química, Cidade Universitária, Campus I, CEP 58059‐900, Jo?o Pessoa, Brazil;3. Embrapa Instrumenta??o Agropecuária, R. XV de Novembro, 1452, S?o Carlos, SP 13560‐9740, Brazil;4. Universidade de S?o Paulo, Instituto de Física de S?o Carlos, Av. Trabalhador S?ocarlense, 400, S?o Carlos, SP 13560‐970, Brazil;5. Embrapa Pecuária Sudeste, Rodovia Washington Luiz, Km 234, Caixa Postal 339, CEP 13560‐970, Brazil |
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| Abstract: | The proline-rich N-terminal domain of gamma-zein has been reported in relevant processes, which include its ability to cross the cell membranes. Evidences indicate that synthetic hexapeptide (PPPVHL), naturally found in N-terminal portion of gamma-zein, can adopt the polyproline II (PPII) conformation in aqueous solution. The secondary structure of gamma-zein in maize protein bodies had been analyzed by solid state Fourier transform infrared and nuclear magnetic resonance spectroscopies. However, it was not possible to measure PPII content in physiological environment since the beta-sheet and PPII signals overlap in both solid state techniques. Here, the secondary structure of gamma-zein has been analyzed by circular dichroism in SDS aqueous solution with and without ditiothreitol (DTT), and in 60% of 2-propanol and water with DTT. The results show that gamma-zein has high helical content in all solutions. The PPII conformation was present at about 7% only in water/DTT solution. |
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| Keywords: | γ‐zein maize prolamin protein secondary structure circular dichroism polyproline II helix |
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