Complexes of Lysine Dendrimer of 2/3 Generations and Semax Peptides. Molecular Dynamics Simulation

نویسندگان

  • IGOR NEELOV
  • ELENA POPOVA
چکیده

Complexes of lysine dendrimer and nootropic Semax peptides were studied using molecular dynamics simulation. These dendrimers were used for drug and other molecules delivery to different cells. It was shown earlier that dendrimers and in particular lysine dendrimers could penetrate blood brain barrier. In present paper three systems containing lysine dendrimers of 2 and 3 generations and 8, 16 or 24 oppositely charged Semax peptides were studied. It was obtained that lysine dendrimers of both generations attracts Semax peptides and forms stable nanocomplexes with peptides. The sizes and structures of these nanocomplexes were investigated. These complexes can be used in future for delivery of Semax peptides to brain since these peptides have significant neuroprotective effects. Key-Words: lysine dendrimer, Semax peptides, computer simulation, molecular dynamics

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Molecular Dynamics Simulation of Interaction of Short Lysine Brush and Oppositely Charged Semax Peptides

The possibility of complex formation by short lysine brush and therapeutic Semax peptides was investigated using molecular dynamics method. Lysine dendrimers and polymer brushes are used for drug and other (e.g., DNA, peptides, and polysaccharides) molecules delivery to different target cells. It is known that they could penetrate blood brain barrier. Since short lysine brush is nontoxic, a sys...

متن کامل

Designing a new tetrapeptide to inhibit the BIR3 domain of the XIAP protein via molecular dynamics simulations

The XIAP protein is a member of apoptosis proteins family. The XIAP protein plays a central role in the inhibition of apoptosis and consists of three Baculoviral IAP Repeat domains. The BIR3 domain binds directly to the N-terminal of caspase-9 and therefore it inhibits apoptosis. N-terminal tetrapeptide region of SMAC protein can bind to BIR3, inhibit it and subsequently induce apoptosis. In th...

متن کامل

How Do Palladium Complexes Affect on Coil Structure of Human Serum Albumin in the Presence of Carbon Nanotube? A Molecular Dynamics Study

To investigate the interaction and adsorption of drug and carbon nanotube on human serum albumin, three anti-cancer drugs ([Pd(phen)(R-gly)]NO3, R = methyl, propyl and amyl) with different hydrophobic tails and anticancer activities were selected. These drugs have better anti-tumor activity and less side effects than that known cis-platinum drug. Human serum albumin is also ...

متن کامل

Interactions of poly(amidoamine) dendrimers with human serum albumin: binding constants and mechanisms.

The interactions of nanomaterials with plasma proteins have a significant impact on their in vivo transport and fate in biological fluids. This article discusses the binding of human serum albumin (HSA) to poly(amidoamine) [PAMAM] dendrimers. We use protein-coated silica particles to measure the HSA binding constants (K(b)) of a homologous series of 19 PAMAM dendrimers in aqueous solutions at p...

متن کامل

Synthesis novel bis-Coumarin derivatives as potential acetylcholinestrase inhibitors: An in vitro, molecular docking, and molecular dynamics simulations study

Alzheimer's disease is an irreversible and progressive brain disorder that slowly destroys memory and thinking skills and ultimately the ability to do the simplest things and can lead to death. Cholinesterases (ChEs) play an important role in controlling cholinergic transmission, and subsequently, by inhibiting CHEs, acetylcholine levels in the brain are elevated. Coumarins have been shown to e...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2017