Modeling interaction between gp120 HIV protein and CCR5 receptor(65 visite) Guryanov I, Real-fernandez F, Sabatino G, Prisco N, Korzhikov-vlakh V, Biondi B, Papini AM, Korzhikova-vlakh E, Rovero P, Tennikova T
Impact factor: 1.807, Impact factor a 5 anni: 1.872
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Parole chiave: Hiv Envelope Protein Gp120 Chemistry Metabolism
, Models, Molecular
, Nanoparticles Chemistry
, Peptides Chemical Synthesis Chemistry
, Receptors, Ccr5 Chemistry Metabolism
, V3 Loop
*** IBB - CNR *** Institute of Chemistry, St. Petersburg State University, St. Petersburg, 198504, Russia. Laboratory of Peptide and Protein Chemistry and Biology, Department of Chemistry "Ugo Schiff", University of Florence, 50019, Sesto Fiorentino, Italy. CNR Istituto di Biostrutture e Bioimmagini, 95126, Catania, Italy. CNR-ICB, Padova Unit, Department of Chemistry, University of Padova, 35131, Padova, Italy. PeptLab@UCP Platform and Laboratory of Chemical Biology EA4505, University Paris-Seine, 95031, Cergy-Pontoise CEDEX, France.
The study of the process of HIV entry into the host cell and the creation of biomimetic nanosystems that are able to selectively bind viral particles and proteins is a high priority research area for the development of novel diagnostic tools and treatment of HIV infection. Recently, we described multilayer nanoparticles (nanotraps) with heparin surface and cationic peptides comprising the N-terminal tail (Nt) and the second extracellular loop (ECL2) of CCR5 receptor, which could bind with high affinity some inflammatory chemokines, in particular, Rantes. Because of the similarity of the binding determinants in CCR5 structure, both for chemokines and gp120 HIV protein, here we expand this approach to the study of the interactions of these biomimetic nanosystems and their components with the peptide representing the V3 loop of the activated form of gp120. According to surface plasmon resonance results, a conformational rearrangement is involved in the process of V3 and CCR5 fragments binding. As in the case of Rantes, ECL2 peptide showed much higher affinity to V3 peptide than Nt (KD = 3.72 x 10(-8) and 1.10 x 10(-6) M, respectively). Heparin-covered nanoparticles bearing CCR5 peptides effectively bound V3 as well. The presence of both heparin and the peptides in the structure of the nanotraps was shown to be crucial for the interaction with the V3 loop. Thus, short cationic peptides ECL2 and Nt proved to be excellent candidates for the design of CCR5 receptor mimetics.<br>
91 Records (83 escludendo Abstract e Conferenze). Impact factor totale: 362.536 (337.765 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 377.122 (347.053 escludendo Abstract e Conferenze).