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Issue 21, 2011
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Exploring the energy landscape of a molecular engineered analog of a tumor-homing peptide

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Abstract

Recently a new non-coded amino acid was designed as a replacement for Arg, to protect the tumor-homing pentapeptide CREKA (Cys-Arg-Glu-Lys-Ala) from proteases. This constrained Arg analog, denoted c5Arg, was engineered to also promote the stability of the CREKA bioactive conformation. The conformational profile of the CREKA analog obtained by replacing Arg by c5Arg has been extensively investigated in this work. Two molecular dynamics simulations-based strategies have been employed: a modified simulated annealing and replica exchange. Results obtained using both techniques show that the conformational features of the new analog fulfill the purpose of its design. The new CREKA analog not only preserves the main structural attributes found for the bioactive conformation of the parent peptide but also shows lower flexibility. Moreover, the conformational profile of the mutated peptide narrows towards the most stable structures previously observed for the parent CREKA peptide.

Graphical abstract: Exploring the energy landscape of a molecular engineered analog of a tumor-homing peptide

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Publication details

The article was received on 17 Nov 2010, accepted on 05 Jan 2011 and first published on 24 Jan 2011


Article type: Paper
DOI: 10.1039/C0CP02572K
Citation: Phys. Chem. Chem. Phys., 2011,13, 9986-9994
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    Exploring the energy landscape of a molecular engineered analog of a tumor-homing peptide

    G. Revilla-López, J. Torras, R. Nussinov, C. Alemán and D. Zanuy, Phys. Chem. Chem. Phys., 2011, 13, 9986
    DOI: 10.1039/C0CP02572K

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