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Modeling of conformational transitions of fibrillogenic peptide, homologous to beta-domain of human alpha-lactalbumin

Abstract

The behavior of the peptide corresponding to beta domain of human alpha-lactalbumin (GYDTQAIVENNESTEYG, WT) has been simulated by the molecular dynamics method. It is shown that, within the model considered, the monomer of this peptide does not tend to form a stable secondary structure; however, simulation of the behavior of several peptide molecules revealed the occurrence of beta structures due to the formation of intermolecular hydrogen bonds. Since the aforementioned interactions involve the terminal portions of peptides, the influence of the tetrapeptide corresponding to the N-terminal portion of WT, TDYG (R), on the secondary structure has been analyzed. The model calculations show that the interaction of this peptide with WT monomer facilitates formation of beta-structures. It is suggested that peptide R may affect the quaternary structure of WT.

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Correspondence to V. V. Kadochnikov.

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Original Russian Text © V.V. Kadochnikov, V.V. Egorov, A.V. Shvetsov, A.I. Kuklin, V.V. Isaev-Ivanov, D.V. Lebedev, 2016, published in Kristallografiya, 2016, Vol. 61, No. 1, pp. 107–114.

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Kadochnikov, V.V., Egorov, V.V., Shvetsov, A.V. et al. Modeling of conformational transitions of fibrillogenic peptide, homologous to beta-domain of human alpha-lactalbumin. Crystallogr. Rep. 61, 98–105 (2016). https://doi.org/10.1134/S1063774516010089

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  • DOI: https://doi.org/10.1134/S1063774516010089

Keywords

  • Fibril
  • Crystallography Report
  • Conformational Transition
  • Beta Structure
  • Fibril Growth